data_9HY3
# 
_entry.id   9HY3 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9HY3         pdb_00009hy3 10.2210/pdb9hy3/pdb 
WWPDB D_1292144451 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-30 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9HY3 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-09 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'sc-4E (scFv derived from the mAb 4E1 against CD93) crystallized at pH 7.5 (monomeric state from gel filtration)' 9HY2 
unspecified 
PDB 'sc-4E (scFv derived from the mAb 4E1 against CD93) crystallized at pH 9.0'                                       9HY5 
unspecified 
PDB 'sc-4E (scFv derived from the mAb 4E1 against CD93) crystallized at pH 7.5 (dimeric state from gel filtration)'   9HY1 
unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              pozzi4@unisi.it 
_pdbx_contact_author.name_first         Cecilia 
_pdbx_contact_author.name_last          Pozzi 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2574-3911 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Raucci, L.'    1 0000-0001-5771-0220 
'Orlandini, M.' 2 0000-0002-6112-4889 
'Pozzi, C.'     3 0000-0003-2574-3911 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Int.J.Biol.Macromol. 
_citation.journal_id_ASTM           IJBMDR 
_citation.journal_id_CSD            0708 
_citation.journal_id_ISSN           0141-8130 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            309 
_citation.language                  ? 
_citation.page_first                143118 
_citation.page_last                 143118 
_citation.title                     
;Structural and antigen-binding surface definition of an anti-CD93 monoclonal antibody for the treatment of degenerative vascular eye diseases.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.ijbiomac.2025.143118 
_citation.pdbx_database_id_PubMed   40228767 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Raucci, L.'    1  ? 
primary 'Perrone, C.D.' 2  ? 
primary 'Barbera, S.'   3  ? 
primary 'de Boer, L.J.' 4  ? 
primary 'Tosi, G.M.'    5  ? 
primary 'Brunetti, J.'  6  ? 
primary 'Bracci, L.'    7  ? 
primary 'Pozzi, C.'     8  ? 
primary 'Galvagni, F.'  9  ? 
primary 'Orlandini, M.' 10 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'sc-4E (scFv derived from the mAb 4E1 against CD93)' 28852.492 1   ? ? ? ? 
2 non-polymer syn 'CHLORIDE ION'                                       35.453    4   ? ? ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                                       62.068    3   ? ? ? ? 
4 non-polymer syn IMIDAZOLE                                            69.085    1   ? ? ? ? 
5 non-polymer syn 'SODIUM ION'                                         22.990    2   ? ? ? ? 
6 water       nat water                                                18.015    334 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MDQEQLQQPGTELVKPGASVRLSCKTSGYTFASYTLHWVKQTPGQGLDWIGAIYPGNGDTSYNQKFKDKATLTADKSSST
AYMQLSNLTSEDSAVYYCARLDWYFDLWGAGTTVTVSAAGGGGSGGGGSGGGGSDIVLTQSPTSLAVSLGQRATISCKAS
QSVDYDGDSYMNWYQQKPGQPPRLLIYAASNLESGIPARFSGSGSGTDFTLNIHPVEEEDAATYYCQQNNEDPRTFGGGT
KLEIKLEMGSSHHHHHHSSGENLYFQGHM
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MDQEQLQQPGTELVKPGASVRLSCKTSGYTFASYTLHWVKQTPGQGLDWIGAIYPGNGDTSYNQKFKDKATLTADKSSST
AYMQLSNLTSEDSAVYYCARLDWYFDLWGAGTTVTVSAAGGGGSGGGGSGGGGSDIVLTQSPTSLAVSLGQRATISCKAS
QSVDYDGDSYMNWYQQKPGQPPRLLIYAASNLESGIPARFSGSGSGTDFTLNIHPVEEEDAATYYCQQNNEDPRTFGGGT
KLEIKLEMGSSHHHHHHSSGENLYFQGHM
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'CHLORIDE ION' CL  
3 1,2-ETHANEDIOL EDO 
4 IMIDAZOLE      IMD 
5 'SODIUM ION'   NA  
6 water          HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ASP n 
1 3   GLN n 
1 4   GLU n 
1 5   GLN n 
1 6   LEU n 
1 7   GLN n 
1 8   GLN n 
1 9   PRO n 
1 10  GLY n 
1 11  THR n 
1 12  GLU n 
1 13  LEU n 
1 14  VAL n 
1 15  LYS n 
1 16  PRO n 
1 17  GLY n 
1 18  ALA n 
1 19  SER n 
1 20  VAL n 
1 21  ARG n 
1 22  LEU n 
1 23  SER n 
1 24  CYS n 
1 25  LYS n 
1 26  THR n 
1 27  SER n 
1 28  GLY n 
1 29  TYR n 
1 30  THR n 
1 31  PHE n 
1 32  ALA n 
1 33  SER n 
1 34  TYR n 
1 35  THR n 
1 36  LEU n 
1 37  HIS n 
1 38  TRP n 
1 39  VAL n 
1 40  LYS n 
1 41  GLN n 
1 42  THR n 
1 43  PRO n 
1 44  GLY n 
1 45  GLN n 
1 46  GLY n 
1 47  LEU n 
1 48  ASP n 
1 49  TRP n 
1 50  ILE n 
1 51  GLY n 
1 52  ALA n 
1 53  ILE n 
1 54  TYR n 
1 55  PRO n 
1 56  GLY n 
1 57  ASN n 
1 58  GLY n 
1 59  ASP n 
1 60  THR n 
1 61  SER n 
1 62  TYR n 
1 63  ASN n 
1 64  GLN n 
1 65  LYS n 
1 66  PHE n 
1 67  LYS n 
1 68  ASP n 
1 69  LYS n 
1 70  ALA n 
1 71  THR n 
1 72  LEU n 
1 73  THR n 
1 74  ALA n 
1 75  ASP n 
1 76  LYS n 
1 77  SER n 
1 78  SER n 
1 79  SER n 
1 80  THR n 
1 81  ALA n 
1 82  TYR n 
1 83  MET n 
1 84  GLN n 
1 85  LEU n 
1 86  SER n 
1 87  ASN n 
1 88  LEU n 
1 89  THR n 
1 90  SER n 
1 91  GLU n 
1 92  ASP n 
1 93  SER n 
1 94  ALA n 
1 95  VAL n 
1 96  TYR n 
1 97  TYR n 
1 98  CYS n 
1 99  ALA n 
1 100 ARG n 
1 101 LEU n 
1 102 ASP n 
1 103 TRP n 
1 104 TYR n 
1 105 PHE n 
1 106 ASP n 
1 107 LEU n 
1 108 TRP n 
1 109 GLY n 
1 110 ALA n 
1 111 GLY n 
1 112 THR n 
1 113 THR n 
1 114 VAL n 
1 115 THR n 
1 116 VAL n 
1 117 SER n 
1 118 ALA n 
1 119 ALA n 
1 120 GLY n 
1 121 GLY n 
1 122 GLY n 
1 123 GLY n 
1 124 SER n 
1 125 GLY n 
1 126 GLY n 
1 127 GLY n 
1 128 GLY n 
1 129 SER n 
1 130 GLY n 
1 131 GLY n 
1 132 GLY n 
1 133 GLY n 
1 134 SER n 
1 135 ASP n 
1 136 ILE n 
1 137 VAL n 
1 138 LEU n 
1 139 THR n 
1 140 GLN n 
1 141 SER n 
1 142 PRO n 
1 143 THR n 
1 144 SER n 
1 145 LEU n 
1 146 ALA n 
1 147 VAL n 
1 148 SER n 
1 149 LEU n 
1 150 GLY n 
1 151 GLN n 
1 152 ARG n 
1 153 ALA n 
1 154 THR n 
1 155 ILE n 
1 156 SER n 
1 157 CYS n 
1 158 LYS n 
1 159 ALA n 
1 160 SER n 
1 161 GLN n 
1 162 SER n 
1 163 VAL n 
1 164 ASP n 
1 165 TYR n 
1 166 ASP n 
1 167 GLY n 
1 168 ASP n 
1 169 SER n 
1 170 TYR n 
1 171 MET n 
1 172 ASN n 
1 173 TRP n 
1 174 TYR n 
1 175 GLN n 
1 176 GLN n 
1 177 LYS n 
1 178 PRO n 
1 179 GLY n 
1 180 GLN n 
1 181 PRO n 
1 182 PRO n 
1 183 ARG n 
1 184 LEU n 
1 185 LEU n 
1 186 ILE n 
1 187 TYR n 
1 188 ALA n 
1 189 ALA n 
1 190 SER n 
1 191 ASN n 
1 192 LEU n 
1 193 GLU n 
1 194 SER n 
1 195 GLY n 
1 196 ILE n 
1 197 PRO n 
1 198 ALA n 
1 199 ARG n 
1 200 PHE n 
1 201 SER n 
1 202 GLY n 
1 203 SER n 
1 204 GLY n 
1 205 SER n 
1 206 GLY n 
1 207 THR n 
1 208 ASP n 
1 209 PHE n 
1 210 THR n 
1 211 LEU n 
1 212 ASN n 
1 213 ILE n 
1 214 HIS n 
1 215 PRO n 
1 216 VAL n 
1 217 GLU n 
1 218 GLU n 
1 219 GLU n 
1 220 ASP n 
1 221 ALA n 
1 222 ALA n 
1 223 THR n 
1 224 TYR n 
1 225 TYR n 
1 226 CYS n 
1 227 GLN n 
1 228 GLN n 
1 229 ASN n 
1 230 ASN n 
1 231 GLU n 
1 232 ASP n 
1 233 PRO n 
1 234 ARG n 
1 235 THR n 
1 236 PHE n 
1 237 GLY n 
1 238 GLY n 
1 239 GLY n 
1 240 THR n 
1 241 LYS n 
1 242 LEU n 
1 243 GLU n 
1 244 ILE n 
1 245 LYS n 
1 246 LEU n 
1 247 GLU n 
1 248 MET n 
1 249 GLY n 
1 250 SER n 
1 251 SER n 
1 252 HIS n 
1 253 HIS n 
1 254 HIS n 
1 255 HIS n 
1 256 HIS n 
1 257 HIS n 
1 258 SER n 
1 259 SER n 
1 260 GLY n 
1 261 GLU n 
1 262 ASN n 
1 263 LEU n 
1 264 TYR n 
1 265 PHE n 
1 266 GLN n 
1 267 GLY n 
1 268 HIS n 
1 269 MET n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   269 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Mus musculus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     10090 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              pLysS 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          Plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET22b(+)' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ?                 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ?                 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ?                 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                 'C4 H7 N O4'     133.103 
CL  non-polymer         . 'CHLORIDE ION'  ?                 'Cl -1'          35.453  
CYS 'L-peptide linking' y CYSTEINE        ?                 'C3 H7 N O2 S'   121.158 
EDO non-polymer         . 1,2-ETHANEDIOL  'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
GLN 'L-peptide linking' y GLUTAMINE       ?                 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ?                 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ?                 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ?                 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ?                 'C6 H13 N O2'    131.173 
IMD non-polymer         . IMIDAZOLE       ?                 'C3 H5 N2 1'     69.085  
LEU 'L-peptide linking' y LEUCINE         ?                 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ?                 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ?                 'C5 H11 N O2 S'  149.211 
NA  non-polymer         . 'SODIUM ION'    ?                 'Na 1'           22.990  
PHE 'L-peptide linking' y PHENYLALANINE   ?                 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ?                 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ?                 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ?                 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ?                 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ?                 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ?                 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   ASP 2   2   ?   ?   ?   A . n 
A 1 3   GLN 3   3   3   GLN GLN A . n 
A 1 4   GLU 4   4   4   GLU GLU A . n 
A 1 5   GLN 5   5   5   GLN GLN A . n 
A 1 6   LEU 6   6   6   LEU LEU A . n 
A 1 7   GLN 7   7   7   GLN GLN A . n 
A 1 8   GLN 8   8   8   GLN GLN A . n 
A 1 9   PRO 9   9   9   PRO PRO A . n 
A 1 10  GLY 10  10  10  GLY GLY A . n 
A 1 11  THR 11  11  11  THR THR A . n 
A 1 12  GLU 12  12  12  GLU GLU A . n 
A 1 13  LEU 13  13  13  LEU LEU A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  LYS 15  15  15  LYS LYS A . n 
A 1 16  PRO 16  16  16  PRO PRO A . n 
A 1 17  GLY 17  17  17  GLY GLY A . n 
A 1 18  ALA 18  18  18  ALA ALA A . n 
A 1 19  SER 19  19  19  SER SER A . n 
A 1 20  VAL 20  20  20  VAL VAL A . n 
A 1 21  ARG 21  21  21  ARG ARG A . n 
A 1 22  LEU 22  22  22  LEU LEU A . n 
A 1 23  SER 23  23  23  SER SER A . n 
A 1 24  CYS 24  24  24  CYS CYS A . n 
A 1 25  LYS 25  25  25  LYS LYS A . n 
A 1 26  THR 26  26  26  THR THR A . n 
A 1 27  SER 27  27  27  SER SER A . n 
A 1 28  GLY 28  28  28  GLY GLY A . n 
A 1 29  TYR 29  29  29  TYR TYR A . n 
A 1 30  THR 30  30  30  THR THR A . n 
A 1 31  PHE 31  31  31  PHE PHE A . n 
A 1 32  ALA 32  32  32  ALA ALA A . n 
A 1 33  SER 33  33  33  SER SER A . n 
A 1 34  TYR 34  34  34  TYR TYR A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  LEU 36  36  36  LEU LEU A . n 
A 1 37  HIS 37  37  37  HIS HIS A . n 
A 1 38  TRP 38  38  38  TRP TRP A . n 
A 1 39  VAL 39  39  39  VAL VAL A . n 
A 1 40  LYS 40  40  40  LYS LYS A . n 
A 1 41  GLN 41  41  41  GLN GLN A . n 
A 1 42  THR 42  42  42  THR THR A . n 
A 1 43  PRO 43  43  43  PRO PRO A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  GLN 45  45  45  GLN GLN A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  TRP 49  49  49  TRP TRP A . n 
A 1 50  ILE 50  50  50  ILE ILE A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  ILE 53  53  53  ILE ILE A . n 
A 1 54  TYR 54  54  54  TYR TYR A . n 
A 1 55  PRO 55  55  55  PRO PRO A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  ASN 57  57  57  ASN ASN A . n 
A 1 58  GLY 58  58  58  GLY GLY A . n 
A 1 59  ASP 59  59  59  ASP ASP A . n 
A 1 60  THR 60  60  60  THR THR A . n 
A 1 61  SER 61  61  61  SER SER A . n 
A 1 62  TYR 62  62  62  TYR TYR A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  GLN 64  64  64  GLN GLN A . n 
A 1 65  LYS 65  65  65  LYS LYS A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  LYS 67  67  67  LYS LYS A . n 
A 1 68  ASP 68  68  68  ASP ASP A . n 
A 1 69  LYS 69  69  69  LYS LYS A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  THR 73  73  73  THR THR A . n 
A 1 74  ALA 74  74  74  ALA ALA A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  SER 77  77  77  SER SER A . n 
A 1 78  SER 78  78  78  SER SER A . n 
A 1 79  SER 79  79  79  SER SER A . n 
A 1 80  THR 80  80  80  THR THR A . n 
A 1 81  ALA 81  81  81  ALA ALA A . n 
A 1 82  TYR 82  82  82  TYR TYR A . n 
A 1 83  MET 83  83  83  MET MET A . n 
A 1 84  GLN 84  84  84  GLN GLN A . n 
A 1 85  LEU 85  85  85  LEU LEU A . n 
A 1 86  SER 86  86  86  SER SER A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  THR 89  89  89  THR THR A . n 
A 1 90  SER 90  90  90  SER SER A . n 
A 1 91  GLU 91  91  91  GLU GLU A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  SER 93  93  93  SER SER A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  TYR 96  96  96  TYR TYR A . n 
A 1 97  TYR 97  97  97  TYR TYR A . n 
A 1 98  CYS 98  98  98  CYS CYS A . n 
A 1 99  ALA 99  99  99  ALA ALA A . n 
A 1 100 ARG 100 100 100 ARG ARG A . n 
A 1 101 LEU 101 101 101 LEU LEU A . n 
A 1 102 ASP 102 102 102 ASP ASP A . n 
A 1 103 TRP 103 103 103 TRP TRP A . n 
A 1 104 TYR 104 104 104 TYR TYR A . n 
A 1 105 PHE 105 105 105 PHE PHE A . n 
A 1 106 ASP 106 106 106 ASP ASP A . n 
A 1 107 LEU 107 107 107 LEU LEU A . n 
A 1 108 TRP 108 108 108 TRP TRP A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 ALA 110 110 110 ALA ALA A . n 
A 1 111 GLY 111 111 111 GLY GLY A . n 
A 1 112 THR 112 112 112 THR THR A . n 
A 1 113 THR 113 113 113 THR THR A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 THR 115 115 115 THR THR A . n 
A 1 116 VAL 116 116 116 VAL VAL A . n 
A 1 117 SER 117 117 117 SER SER A . n 
A 1 118 ALA 118 118 118 ALA ALA A . n 
A 1 119 ALA 119 119 119 ALA ALA A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 GLY 121 121 ?   ?   ?   A . n 
A 1 122 GLY 122 122 ?   ?   ?   A . n 
A 1 123 GLY 123 123 ?   ?   ?   A . n 
A 1 124 SER 124 124 ?   ?   ?   A . n 
A 1 125 GLY 125 125 ?   ?   ?   A . n 
A 1 126 GLY 126 126 ?   ?   ?   A . n 
A 1 127 GLY 127 127 ?   ?   ?   A . n 
A 1 128 GLY 128 128 ?   ?   ?   A . n 
A 1 129 SER 129 129 ?   ?   ?   A . n 
A 1 130 GLY 130 130 ?   ?   ?   A . n 
A 1 131 GLY 131 131 ?   ?   ?   A . n 
A 1 132 GLY 132 132 ?   ?   ?   A . n 
A 1 133 GLY 133 133 ?   ?   ?   A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 ILE 136 136 136 ILE ILE A . n 
A 1 137 VAL 137 137 137 VAL VAL A . n 
A 1 138 LEU 138 138 138 LEU LEU A . n 
A 1 139 THR 139 139 139 THR THR A . n 
A 1 140 GLN 140 140 140 GLN GLN A . n 
A 1 141 SER 141 141 141 SER SER A . n 
A 1 142 PRO 142 142 142 PRO PRO A . n 
A 1 143 THR 143 143 143 THR THR A . n 
A 1 144 SER 144 144 144 SER SER A . n 
A 1 145 LEU 145 145 145 LEU LEU A . n 
A 1 146 ALA 146 146 146 ALA ALA A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 SER 148 148 148 SER SER A . n 
A 1 149 LEU 149 149 149 LEU LEU A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 GLN 151 151 151 GLN GLN A . n 
A 1 152 ARG 152 152 152 ARG ARG A . n 
A 1 153 ALA 153 153 153 ALA ALA A . n 
A 1 154 THR 154 154 154 THR THR A . n 
A 1 155 ILE 155 155 155 ILE ILE A . n 
A 1 156 SER 156 156 156 SER SER A . n 
A 1 157 CYS 157 157 157 CYS CYS A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ALA 159 159 159 ALA ALA A . n 
A 1 160 SER 160 160 160 SER SER A . n 
A 1 161 GLN 161 161 161 GLN GLN A . n 
A 1 162 SER 162 162 162 SER SER A . n 
A 1 163 VAL 163 163 163 VAL VAL A . n 
A 1 164 ASP 164 164 164 ASP ASP A . n 
A 1 165 TYR 165 165 165 TYR TYR A . n 
A 1 166 ASP 166 166 166 ASP ASP A . n 
A 1 167 GLY 167 167 167 GLY GLY A . n 
A 1 168 ASP 168 168 168 ASP ASP A . n 
A 1 169 SER 169 169 169 SER SER A . n 
A 1 170 TYR 170 170 170 TYR TYR A . n 
A 1 171 MET 171 171 171 MET MET A . n 
A 1 172 ASN 172 172 172 ASN ASN A . n 
A 1 173 TRP 173 173 173 TRP TRP A . n 
A 1 174 TYR 174 174 174 TYR TYR A . n 
A 1 175 GLN 175 175 175 GLN GLN A . n 
A 1 176 GLN 176 176 176 GLN GLN A . n 
A 1 177 LYS 177 177 177 LYS LYS A . n 
A 1 178 PRO 178 178 178 PRO PRO A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 GLN 180 180 180 GLN GLN A . n 
A 1 181 PRO 181 181 181 PRO PRO A . n 
A 1 182 PRO 182 182 182 PRO PRO A . n 
A 1 183 ARG 183 183 183 ARG ARG A . n 
A 1 184 LEU 184 184 184 LEU LEU A . n 
A 1 185 LEU 185 185 185 LEU LEU A . n 
A 1 186 ILE 186 186 186 ILE ILE A . n 
A 1 187 TYR 187 187 187 TYR TYR A . n 
A 1 188 ALA 188 188 188 ALA ALA A . n 
A 1 189 ALA 189 189 189 ALA ALA A . n 
A 1 190 SER 190 190 190 SER SER A . n 
A 1 191 ASN 191 191 191 ASN ASN A . n 
A 1 192 LEU 192 192 192 LEU LEU A . n 
A 1 193 GLU 193 193 193 GLU GLU A . n 
A 1 194 SER 194 194 194 SER SER A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 ILE 196 196 196 ILE ILE A . n 
A 1 197 PRO 197 197 197 PRO PRO A . n 
A 1 198 ALA 198 198 198 ALA ALA A . n 
A 1 199 ARG 199 199 199 ARG ARG A . n 
A 1 200 PHE 200 200 200 PHE PHE A . n 
A 1 201 SER 201 201 201 SER SER A . n 
A 1 202 GLY 202 202 202 GLY GLY A . n 
A 1 203 SER 203 203 203 SER SER A . n 
A 1 204 GLY 204 204 204 GLY GLY A . n 
A 1 205 SER 205 205 205 SER SER A . n 
A 1 206 GLY 206 206 206 GLY GLY A . n 
A 1 207 THR 207 207 207 THR THR A . n 
A 1 208 ASP 208 208 208 ASP ASP A . n 
A 1 209 PHE 209 209 209 PHE PHE A . n 
A 1 210 THR 210 210 210 THR THR A . n 
A 1 211 LEU 211 211 211 LEU LEU A . n 
A 1 212 ASN 212 212 212 ASN ASN A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 HIS 214 214 214 HIS HIS A . n 
A 1 215 PRO 215 215 215 PRO PRO A . n 
A 1 216 VAL 216 216 216 VAL VAL A . n 
A 1 217 GLU 217 217 217 GLU GLU A . n 
A 1 218 GLU 218 218 218 GLU GLU A . n 
A 1 219 GLU 219 219 219 GLU GLU A . n 
A 1 220 ASP 220 220 220 ASP ASP A . n 
A 1 221 ALA 221 221 221 ALA ALA A . n 
A 1 222 ALA 222 222 222 ALA ALA A . n 
A 1 223 THR 223 223 223 THR THR A . n 
A 1 224 TYR 224 224 224 TYR TYR A . n 
A 1 225 TYR 225 225 225 TYR TYR A . n 
A 1 226 CYS 226 226 226 CYS CYS A . n 
A 1 227 GLN 227 227 227 GLN GLN A . n 
A 1 228 GLN 228 228 228 GLN GLN A . n 
A 1 229 ASN 229 229 229 ASN ASN A . n 
A 1 230 ASN 230 230 230 ASN ASN A . n 
A 1 231 GLU 231 231 231 GLU GLU A . n 
A 1 232 ASP 232 232 232 ASP ASP A . n 
A 1 233 PRO 233 233 233 PRO PRO A . n 
A 1 234 ARG 234 234 234 ARG ARG A . n 
A 1 235 THR 235 235 235 THR THR A . n 
A 1 236 PHE 236 236 236 PHE PHE A . n 
A 1 237 GLY 237 237 237 GLY GLY A . n 
A 1 238 GLY 238 238 238 GLY GLY A . n 
A 1 239 GLY 239 239 239 GLY GLY A . n 
A 1 240 THR 240 240 240 THR THR A . n 
A 1 241 LYS 241 241 241 LYS LYS A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 GLU 243 243 243 GLU GLU A . n 
A 1 244 ILE 244 244 244 ILE ILE A . n 
A 1 245 LYS 245 245 245 LYS LYS A . n 
A 1 246 LEU 246 246 246 LEU LEU A . n 
A 1 247 GLU 247 247 247 GLU GLU A . n 
A 1 248 MET 248 248 ?   ?   ?   A . n 
A 1 249 GLY 249 249 ?   ?   ?   A . n 
A 1 250 SER 250 250 ?   ?   ?   A . n 
A 1 251 SER 251 251 ?   ?   ?   A . n 
A 1 252 HIS 252 252 ?   ?   ?   A . n 
A 1 253 HIS 253 253 ?   ?   ?   A . n 
A 1 254 HIS 254 254 ?   ?   ?   A . n 
A 1 255 HIS 255 255 ?   ?   ?   A . n 
A 1 256 HIS 256 256 ?   ?   ?   A . n 
A 1 257 HIS 257 257 ?   ?   ?   A . n 
A 1 258 SER 258 258 ?   ?   ?   A . n 
A 1 259 SER 259 259 ?   ?   ?   A . n 
A 1 260 GLY 260 260 ?   ?   ?   A . n 
A 1 261 GLU 261 261 ?   ?   ?   A . n 
A 1 262 ASN 262 262 ?   ?   ?   A . n 
A 1 263 LEU 263 263 ?   ?   ?   A . n 
A 1 264 TYR 264 264 ?   ?   ?   A . n 
A 1 265 PHE 265 265 ?   ?   ?   A . n 
A 1 266 GLN 266 266 ?   ?   ?   A . n 
A 1 267 GLY 267 267 ?   ?   ?   A . n 
A 1 268 HIS 268 268 ?   ?   ?   A . n 
A 1 269 MET 269 269 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        NA 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   NA 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 CL  1   301 300 CL  CL  A . 
C 3 EDO 1   302 301 EDO EDO A . 
D 3 EDO 1   303 302 EDO EDO A . 
E 4 IMD 1   304 303 IMD IMD A . 
F 3 EDO 1   305 304 EDO EDO A . 
G 5 NA  1   306 1   NA  NA  A . 
H 5 NA  1   307 2   NA  NA  A . 
I 2 CL  1   308 1   CL  CL  A . 
J 2 CL  1   309 2   CL  CL  A . 
K 2 CL  1   310 3   CL  CL  A . 
L 6 HOH 1   401 201 HOH HOH A . 
L 6 HOH 2   402 359 HOH HOH A . 
L 6 HOH 3   403 304 HOH HOH A . 
L 6 HOH 4   404 407 HOH HOH A . 
L 6 HOH 5   405 160 HOH HOH A . 
L 6 HOH 6   406 409 HOH HOH A . 
L 6 HOH 7   407 192 HOH HOH A . 
L 6 HOH 8   408 427 HOH HOH A . 
L 6 HOH 9   409 9   HOH HOH A . 
L 6 HOH 10  410 439 HOH HOH A . 
L 6 HOH 11  411 122 HOH HOH A . 
L 6 HOH 12  412 83  HOH HOH A . 
L 6 HOH 13  413 134 HOH HOH A . 
L 6 HOH 14  414 309 HOH HOH A . 
L 6 HOH 15  415 52  HOH HOH A . 
L 6 HOH 16  416 365 HOH HOH A . 
L 6 HOH 17  417 249 HOH HOH A . 
L 6 HOH 18  418 369 HOH HOH A . 
L 6 HOH 19  419 306 HOH HOH A . 
L 6 HOH 20  420 47  HOH HOH A . 
L 6 HOH 21  421 149 HOH HOH A . 
L 6 HOH 22  422 444 HOH HOH A . 
L 6 HOH 23  423 227 HOH HOH A . 
L 6 HOH 24  424 360 HOH HOH A . 
L 6 HOH 25  425 326 HOH HOH A . 
L 6 HOH 26  426 267 HOH HOH A . 
L 6 HOH 27  427 287 HOH HOH A . 
L 6 HOH 28  428 37  HOH HOH A . 
L 6 HOH 29  429 51  HOH HOH A . 
L 6 HOH 30  430 107 HOH HOH A . 
L 6 HOH 31  431 368 HOH HOH A . 
L 6 HOH 32  432 6   HOH HOH A . 
L 6 HOH 33  433 226 HOH HOH A . 
L 6 HOH 34  434 305 HOH HOH A . 
L 6 HOH 35  435 180 HOH HOH A . 
L 6 HOH 36  436 113 HOH HOH A . 
L 6 HOH 37  437 66  HOH HOH A . 
L 6 HOH 38  438 153 HOH HOH A . 
L 6 HOH 39  439 339 HOH HOH A . 
L 6 HOH 40  440 366 HOH HOH A . 
L 6 HOH 41  441 471 HOH HOH A . 
L 6 HOH 42  442 167 HOH HOH A . 
L 6 HOH 43  443 143 HOH HOH A . 
L 6 HOH 44  444 259 HOH HOH A . 
L 6 HOH 45  445 424 HOH HOH A . 
L 6 HOH 46  446 169 HOH HOH A . 
L 6 HOH 47  447 254 HOH HOH A . 
L 6 HOH 48  448 320 HOH HOH A . 
L 6 HOH 49  449 18  HOH HOH A . 
L 6 HOH 50  450 236 HOH HOH A . 
L 6 HOH 51  451 362 HOH HOH A . 
L 6 HOH 52  452 141 HOH HOH A . 
L 6 HOH 53  453 4   HOH HOH A . 
L 6 HOH 54  454 103 HOH HOH A . 
L 6 HOH 55  455 73  HOH HOH A . 
L 6 HOH 56  456 12  HOH HOH A . 
L 6 HOH 57  457 210 HOH HOH A . 
L 6 HOH 58  458 65  HOH HOH A . 
L 6 HOH 59  459 162 HOH HOH A . 
L 6 HOH 60  460 220 HOH HOH A . 
L 6 HOH 61  461 224 HOH HOH A . 
L 6 HOH 62  462 154 HOH HOH A . 
L 6 HOH 63  463 53  HOH HOH A . 
L 6 HOH 64  464 111 HOH HOH A . 
L 6 HOH 65  465 70  HOH HOH A . 
L 6 HOH 66  466 88  HOH HOH A . 
L 6 HOH 67  467 239 HOH HOH A . 
L 6 HOH 68  468 84  HOH HOH A . 
L 6 HOH 69  469 145 HOH HOH A . 
L 6 HOH 70  470 419 HOH HOH A . 
L 6 HOH 71  471 81  HOH HOH A . 
L 6 HOH 72  472 418 HOH HOH A . 
L 6 HOH 73  473 382 HOH HOH A . 
L 6 HOH 74  474 255 HOH HOH A . 
L 6 HOH 75  475 198 HOH HOH A . 
L 6 HOH 76  476 89  HOH HOH A . 
L 6 HOH 77  477 130 HOH HOH A . 
L 6 HOH 78  478 195 HOH HOH A . 
L 6 HOH 79  479 312 HOH HOH A . 
L 6 HOH 80  480 95  HOH HOH A . 
L 6 HOH 81  481 207 HOH HOH A . 
L 6 HOH 82  482 148 HOH HOH A . 
L 6 HOH 83  483 60  HOH HOH A . 
L 6 HOH 84  484 74  HOH HOH A . 
L 6 HOH 85  485 373 HOH HOH A . 
L 6 HOH 86  486 14  HOH HOH A . 
L 6 HOH 87  487 123 HOH HOH A . 
L 6 HOH 88  488 186 HOH HOH A . 
L 6 HOH 89  489 41  HOH HOH A . 
L 6 HOH 90  490 412 HOH HOH A . 
L 6 HOH 91  491 72  HOH HOH A . 
L 6 HOH 92  492 202 HOH HOH A . 
L 6 HOH 93  493 48  HOH HOH A . 
L 6 HOH 94  494 54  HOH HOH A . 
L 6 HOH 95  495 189 HOH HOH A . 
L 6 HOH 96  496 393 HOH HOH A . 
L 6 HOH 97  497 45  HOH HOH A . 
L 6 HOH 98  498 71  HOH HOH A . 
L 6 HOH 99  499 434 HOH HOH A . 
L 6 HOH 100 500 414 HOH HOH A . 
L 6 HOH 101 501 136 HOH HOH A . 
L 6 HOH 102 502 121 HOH HOH A . 
L 6 HOH 103 503 191 HOH HOH A . 
L 6 HOH 104 504 55  HOH HOH A . 
L 6 HOH 105 505 172 HOH HOH A . 
L 6 HOH 106 506 238 HOH HOH A . 
L 6 HOH 107 507 386 HOH HOH A . 
L 6 HOH 108 508 318 HOH HOH A . 
L 6 HOH 109 509 146 HOH HOH A . 
L 6 HOH 110 510 375 HOH HOH A . 
L 6 HOH 111 511 164 HOH HOH A . 
L 6 HOH 112 512 77  HOH HOH A . 
L 6 HOH 113 513 135 HOH HOH A . 
L 6 HOH 114 514 243 HOH HOH A . 
L 6 HOH 115 515 397 HOH HOH A . 
L 6 HOH 116 516 56  HOH HOH A . 
L 6 HOH 117 517 91  HOH HOH A . 
L 6 HOH 118 518 376 HOH HOH A . 
L 6 HOH 119 519 370 HOH HOH A . 
L 6 HOH 120 520 140 HOH HOH A . 
L 6 HOH 121 521 100 HOH HOH A . 
L 6 HOH 122 522 214 HOH HOH A . 
L 6 HOH 123 523 371 HOH HOH A . 
L 6 HOH 124 524 398 HOH HOH A . 
L 6 HOH 125 525 187 HOH HOH A . 
L 6 HOH 126 526 87  HOH HOH A . 
L 6 HOH 127 527 116 HOH HOH A . 
L 6 HOH 128 528 86  HOH HOH A . 
L 6 HOH 129 529 436 HOH HOH A . 
L 6 HOH 130 530 110 HOH HOH A . 
L 6 HOH 131 531 104 HOH HOH A . 
L 6 HOH 132 532 61  HOH HOH A . 
L 6 HOH 133 533 69  HOH HOH A . 
L 6 HOH 134 534 97  HOH HOH A . 
L 6 HOH 135 535 39  HOH HOH A . 
L 6 HOH 136 536 82  HOH HOH A . 
L 6 HOH 137 537 17  HOH HOH A . 
L 6 HOH 138 538 361 HOH HOH A . 
L 6 HOH 139 539 392 HOH HOH A . 
L 6 HOH 140 540 32  HOH HOH A . 
L 6 HOH 141 541 385 HOH HOH A . 
L 6 HOH 142 542 257 HOH HOH A . 
L 6 HOH 143 543 228 HOH HOH A . 
L 6 HOH 144 544 211 HOH HOH A . 
L 6 HOH 145 545 101 HOH HOH A . 
L 6 HOH 146 546 35  HOH HOH A . 
L 6 HOH 147 547 42  HOH HOH A . 
L 6 HOH 148 548 108 HOH HOH A . 
L 6 HOH 149 549 387 HOH HOH A . 
L 6 HOH 150 550 262 HOH HOH A . 
L 6 HOH 151 551 279 HOH HOH A . 
L 6 HOH 152 552 105 HOH HOH A . 
L 6 HOH 153 553 470 HOH HOH A . 
L 6 HOH 154 554 24  HOH HOH A . 
L 6 HOH 155 555 152 HOH HOH A . 
L 6 HOH 156 556 62  HOH HOH A . 
L 6 HOH 157 557 131 HOH HOH A . 
L 6 HOH 158 558 119 HOH HOH A . 
L 6 HOH 159 559 115 HOH HOH A . 
L 6 HOH 160 560 199 HOH HOH A . 
L 6 HOH 161 561 161 HOH HOH A . 
L 6 HOH 162 562 64  HOH HOH A . 
L 6 HOH 163 563 388 HOH HOH A . 
L 6 HOH 164 564 394 HOH HOH A . 
L 6 HOH 165 565 170 HOH HOH A . 
L 6 HOH 166 566 156 HOH HOH A . 
L 6 HOH 167 567 118 HOH HOH A . 
L 6 HOH 168 568 413 HOH HOH A . 
L 6 HOH 169 569 16  HOH HOH A . 
L 6 HOH 170 570 352 HOH HOH A . 
L 6 HOH 171 571 68  HOH HOH A . 
L 6 HOH 172 572 138 HOH HOH A . 
L 6 HOH 173 573 429 HOH HOH A . 
L 6 HOH 174 574 281 HOH HOH A . 
L 6 HOH 175 575 319 HOH HOH A . 
L 6 HOH 176 576 231 HOH HOH A . 
L 6 HOH 177 577 94  HOH HOH A . 
L 6 HOH 178 578 237 HOH HOH A . 
L 6 HOH 179 579 30  HOH HOH A . 
L 6 HOH 180 580 31  HOH HOH A . 
L 6 HOH 181 581 102 HOH HOH A . 
L 6 HOH 182 582 15  HOH HOH A . 
L 6 HOH 183 583 106 HOH HOH A . 
L 6 HOH 184 584 23  HOH HOH A . 
L 6 HOH 185 585 127 HOH HOH A . 
L 6 HOH 186 586 428 HOH HOH A . 
L 6 HOH 187 587 311 HOH HOH A . 
L 6 HOH 188 588 215 HOH HOH A . 
L 6 HOH 189 589 396 HOH HOH A . 
L 6 HOH 190 590 46  HOH HOH A . 
L 6 HOH 191 591 159 HOH HOH A . 
L 6 HOH 192 592 25  HOH HOH A . 
L 6 HOH 193 593 22  HOH HOH A . 
L 6 HOH 194 594 3   HOH HOH A . 
L 6 HOH 195 595 302 HOH HOH A . 
L 6 HOH 196 596 58  HOH HOH A . 
L 6 HOH 197 597 270 HOH HOH A . 
L 6 HOH 198 598 379 HOH HOH A . 
L 6 HOH 199 599 403 HOH HOH A . 
L 6 HOH 200 600 203 HOH HOH A . 
L 6 HOH 201 601 158 HOH HOH A . 
L 6 HOH 202 602 354 HOH HOH A . 
L 6 HOH 203 603 408 HOH HOH A . 
L 6 HOH 204 604 80  HOH HOH A . 
L 6 HOH 205 605 363 HOH HOH A . 
L 6 HOH 206 606 221 HOH HOH A . 
L 6 HOH 207 607 364 HOH HOH A . 
L 6 HOH 208 608 330 HOH HOH A . 
L 6 HOH 209 609 49  HOH HOH A . 
L 6 HOH 210 610 461 HOH HOH A . 
L 6 HOH 211 611 209 HOH HOH A . 
L 6 HOH 212 612 144 HOH HOH A . 
L 6 HOH 213 613 400 HOH HOH A . 
L 6 HOH 214 614 463 HOH HOH A . 
L 6 HOH 215 615 11  HOH HOH A . 
L 6 HOH 216 616 50  HOH HOH A . 
L 6 HOH 217 617 142 HOH HOH A . 
L 6 HOH 218 618 99  HOH HOH A . 
L 6 HOH 219 619 5   HOH HOH A . 
L 6 HOH 220 620 399 HOH HOH A . 
L 6 HOH 221 621 8   HOH HOH A . 
L 6 HOH 222 622 21  HOH HOH A . 
L 6 HOH 223 623 19  HOH HOH A . 
L 6 HOH 224 624 75  HOH HOH A . 
L 6 HOH 225 625 456 HOH HOH A . 
L 6 HOH 226 626 20  HOH HOH A . 
L 6 HOH 227 627 421 HOH HOH A . 
L 6 HOH 228 628 462 HOH HOH A . 
L 6 HOH 229 629 90  HOH HOH A . 
L 6 HOH 230 630 383 HOH HOH A . 
L 6 HOH 231 631 40  HOH HOH A . 
L 6 HOH 232 632 57  HOH HOH A . 
L 6 HOH 233 633 44  HOH HOH A . 
L 6 HOH 234 634 205 HOH HOH A . 
L 6 HOH 235 635 244 HOH HOH A . 
L 6 HOH 236 636 391 HOH HOH A . 
L 6 HOH 237 637 179 HOH HOH A . 
L 6 HOH 238 638 33  HOH HOH A . 
L 6 HOH 239 639 38  HOH HOH A . 
L 6 HOH 240 640 395 HOH HOH A . 
L 6 HOH 241 641 261 HOH HOH A . 
L 6 HOH 242 642 34  HOH HOH A . 
L 6 HOH 243 643 36  HOH HOH A . 
L 6 HOH 244 644 310 HOH HOH A . 
L 6 HOH 245 645 185 HOH HOH A . 
L 6 HOH 246 646 380 HOH HOH A . 
L 6 HOH 247 647 28  HOH HOH A . 
L 6 HOH 248 648 163 HOH HOH A . 
L 6 HOH 249 649 133 HOH HOH A . 
L 6 HOH 250 650 128 HOH HOH A . 
L 6 HOH 251 651 406 HOH HOH A . 
L 6 HOH 252 652 467 HOH HOH A . 
L 6 HOH 253 653 93  HOH HOH A . 
L 6 HOH 254 654 472 HOH HOH A . 
L 6 HOH 255 655 435 HOH HOH A . 
L 6 HOH 256 656 177 HOH HOH A . 
L 6 HOH 257 657 120 HOH HOH A . 
L 6 HOH 258 658 245 HOH HOH A . 
L 6 HOH 259 659 125 HOH HOH A . 
L 6 HOH 260 660 193 HOH HOH A . 
L 6 HOH 261 661 258 HOH HOH A . 
L 6 HOH 262 662 63  HOH HOH A . 
L 6 HOH 263 663 230 HOH HOH A . 
L 6 HOH 264 664 450 HOH HOH A . 
L 6 HOH 265 665 323 HOH HOH A . 
L 6 HOH 266 666 351 HOH HOH A . 
L 6 HOH 267 667 165 HOH HOH A . 
L 6 HOH 268 668 465 HOH HOH A . 
L 6 HOH 269 669 27  HOH HOH A . 
L 6 HOH 270 670 263 HOH HOH A . 
L 6 HOH 271 671 43  HOH HOH A . 
L 6 HOH 272 672 188 HOH HOH A . 
L 6 HOH 273 673 384 HOH HOH A . 
L 6 HOH 274 674 208 HOH HOH A . 
L 6 HOH 275 675 7   HOH HOH A . 
L 6 HOH 276 676 109 HOH HOH A . 
L 6 HOH 277 677 129 HOH HOH A . 
L 6 HOH 278 678 464 HOH HOH A . 
L 6 HOH 279 679 59  HOH HOH A . 
L 6 HOH 280 680 79  HOH HOH A . 
L 6 HOH 281 681 473 HOH HOH A . 
L 6 HOH 282 682 132 HOH HOH A . 
L 6 HOH 283 683 289 HOH HOH A . 
L 6 HOH 284 684 241 HOH HOH A . 
L 6 HOH 285 685 85  HOH HOH A . 
L 6 HOH 286 686 381 HOH HOH A . 
L 6 HOH 287 687 313 HOH HOH A . 
L 6 HOH 288 688 10  HOH HOH A . 
L 6 HOH 289 689 176 HOH HOH A . 
L 6 HOH 290 690 468 HOH HOH A . 
L 6 HOH 291 691 353 HOH HOH A . 
L 6 HOH 292 692 327 HOH HOH A . 
L 6 HOH 293 693 184 HOH HOH A . 
L 6 HOH 294 694 433 HOH HOH A . 
L 6 HOH 295 695 137 HOH HOH A . 
L 6 HOH 296 696 150 HOH HOH A . 
L 6 HOH 297 697 13  HOH HOH A . 
L 6 HOH 298 698 242 HOH HOH A . 
L 6 HOH 299 699 76  HOH HOH A . 
L 6 HOH 300 700 355 HOH HOH A . 
L 6 HOH 301 701 29  HOH HOH A . 
L 6 HOH 302 702 372 HOH HOH A . 
L 6 HOH 303 703 443 HOH HOH A . 
L 6 HOH 304 704 401 HOH HOH A . 
L 6 HOH 305 705 420 HOH HOH A . 
L 6 HOH 306 706 442 HOH HOH A . 
L 6 HOH 307 707 114 HOH HOH A . 
L 6 HOH 308 708 358 HOH HOH A . 
L 6 HOH 309 709 410 HOH HOH A . 
L 6 HOH 310 710 367 HOH HOH A . 
L 6 HOH 311 711 333 HOH HOH A . 
L 6 HOH 312 712 389 HOH HOH A . 
L 6 HOH 313 713 92  HOH HOH A . 
L 6 HOH 314 714 246 HOH HOH A . 
L 6 HOH 315 715 157 HOH HOH A . 
L 6 HOH 316 716 374 HOH HOH A . 
L 6 HOH 317 717 139 HOH HOH A . 
L 6 HOH 318 718 269 HOH HOH A . 
L 6 HOH 319 719 166 HOH HOH A . 
L 6 HOH 320 720 219 HOH HOH A . 
L 6 HOH 321 721 98  HOH HOH A . 
L 6 HOH 322 722 181 HOH HOH A . 
L 6 HOH 323 723 112 HOH HOH A . 
L 6 HOH 324 724 222 HOH HOH A . 
L 6 HOH 325 725 404 HOH HOH A . 
L 6 HOH 326 726 182 HOH HOH A . 
L 6 HOH 327 727 168 HOH HOH A . 
L 6 HOH 328 728 437 HOH HOH A . 
L 6 HOH 329 729 178 HOH HOH A . 
L 6 HOH 330 730 390 HOH HOH A . 
L 6 HOH 331 731 96  HOH HOH A . 
L 6 HOH 332 732 183 HOH HOH A . 
L 6 HOH 333 733 273 HOH HOH A . 
L 6 HOH 334 734 469 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLN 3   ? CG  ? A GLN 3   CG  
2  1 Y 1 A GLN 3   ? CD  ? A GLN 3   CD  
3  1 Y 1 A GLN 3   ? OE1 ? A GLN 3   OE1 
4  1 Y 1 A GLN 3   ? NE2 ? A GLN 3   NE2 
5  1 Y 1 A LYS 25  ? CE  ? A LYS 25  CE  
6  1 Y 1 A LYS 25  ? NZ  ? A LYS 25  NZ  
7  1 Y 1 A GLN 64  ? CD  ? A GLN 64  CD  
8  1 Y 1 A GLN 64  ? OE1 ? A GLN 64  OE1 
9  1 Y 1 A GLN 64  ? NE2 ? A GLN 64  NE2 
10 1 Y 1 A LYS 67  ? CD  ? A LYS 67  CD  
11 1 Y 1 A LYS 67  ? CE  ? A LYS 67  CE  
12 1 Y 1 A LYS 67  ? NZ  ? A LYS 67  NZ  
13 1 Y 1 A GLU 247 ? CG  ? A GLU 247 CG  
14 1 Y 1 A GLU 247 ? CD  ? A GLU 247 CD  
15 1 Y 1 A GLU 247 ? OE1 ? A GLU 247 OE1 
16 1 Y 1 A GLU 247 ? OE2 ? A GLU 247 OE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0425 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP  ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9HY3 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     64.531 
_cell.length_a_esd                 ? 
_cell.length_b                     64.531 
_cell.length_b_esd                 ? 
_cell.length_c                     160.509 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9HY3 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                154 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 32 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9HY3 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.19 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          61.44 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              5.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    'room temperature' 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '4.3 M NaCl, 0.1 M bis-tris pH 5.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-09-20 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    'Si(111)' 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97626 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97626 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate                          30.5 
_reflns.entry_id                                       9HY3 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.62 
_reflns.d_resolution_low                               52.78 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     49253 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                8.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.07 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.078 
_reflns.pdbx_Rpim_I_all                                0.026 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.073 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.62 
_reflns_shell.d_res_low                                     1.65 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.2 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2457 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               9.0 
_reflns_shell.pdbx_chi_squared                              0.69 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               1.041 
_reflns_shell.pdbx_Rpim_I_all                               0.344 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.584 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.981 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.01 
_refine.aniso_B[1][2]                            0.01 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            0.01 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -0.03 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               34.658 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.976 
_refine.correlation_coeff_Fo_to_Fc_free          0.966 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9HY3 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.62 
_refine.ls_d_res_low                             52.78 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     46242 
_refine.ls_number_reflns_R_free                  2461 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.04 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.17687 
_refine.ls_R_factor_R_free                       0.20673 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.17534 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.070 
_refine.pdbx_overall_ESU_R_Free                  0.075 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             3.812 
_refine.overall_SU_ML                            0.063 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_analyze.entry_id                        9HY3 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.25 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.62 
_refine_hist.d_res_low                        52.78 
_refine_hist.number_atoms_solvent             334 
_refine_hist.number_atoms_total               2119 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1762 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         23 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.011  0.012  1870 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 2.022  1.802  2532 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.127  5.000  242  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 5.962  5.000  7    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 11.015 10.000 281  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.153  0.200  275  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.012  0.020  1463 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 2.297  2.213  941  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 3.141  3.950  1177 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.544  2.450  929  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 7.083  28.22  2893 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.620 
_refine_ls_shell.d_res_low                        1.662 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             201 
_refine_ls_shell.number_reflns_R_work             3443 
_refine_ls_shell.percent_reflns_obs               99.21 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.432 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.454 
# 
_struct.entry_id                     9HY3 
_struct.title                        'sc-4E (scFv derived from the mAb 4E1 against CD93) crystallized at pH 5.5' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9HY3 
_struct_keywords.text            'single-chain antibody fragment, scFv, monoclonal antibody 4E1 against CD93, sc-4E, IMMUNE SYSTEM' 
_struct_keywords.pdbx_keywords   'IMMUNE SYSTEM' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 4 ? 
F N N 3 ? 
G N N 5 ? 
H N N 5 ? 
I N N 2 ? 
J N N 2 ? 
K N N 2 ? 
L N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    9HY3 
_struct_ref.pdbx_db_accession          9HY3 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9HY3 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 269 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             9HY3 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  269 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       269 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1450  ? 
1 MORE         -37   ? 
1 'SSA (A^2)'  11110 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                'monomeric state sample in solution (obtained from gel filtration)' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 THR A 30  ? TYR A 34  ? THR A 30  TYR A 34  5 ? 5 
HELX_P HELX_P2 AA2 GLN A 64  ? LYS A 67  ? GLN A 64  LYS A 67  5 ? 4 
HELX_P HELX_P3 AA3 LYS A 76  ? SER A 78  ? LYS A 76  SER A 78  5 ? 3 
HELX_P HELX_P4 AA4 THR A 89  ? SER A 93  ? THR A 89  SER A 93  5 ? 5 
HELX_P HELX_P5 AA5 ASP A 102 ? ASP A 106 ? ASP A 102 ASP A 106 5 ? 5 
HELX_P HELX_P6 AA6 GLU A 217 ? ALA A 221 ? GLU A 217 ALA A 221 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? A CYS 24  SG ? ? ? 1_555 A CYS 98  SG ? ? A CYS 24  A CYS 98  1_555 ? ? ? ? ? ? ? 2.251 ? ? 
disulf2  disulf ? ? A CYS 157 SG ? ? ? 1_555 A CYS 226 SG ? ? A CYS 157 A CYS 226 1_555 ? ? ? ? ? ? ? 2.463 ? ? 
metalc1  metalc ? ? A SER 79  OG ? ? ? 1_555 G NA  .   NA ? ? A SER 79  A NA  306 1_555 ? ? ? ? ? ? ? 2.427 ? ? 
metalc2  metalc ? ? A TYR 104 O  ? ? ? 1_555 H NA  .   NA ? ? A TYR 104 A NA  307 4_565 ? ? ? ? ? ? ? 2.501 ? ? 
metalc3  metalc ? ? A SER 141 OG ? ? ? 1_555 H NA  .   NA ? ? A SER 141 A NA  307 1_555 ? ? ? ? ? ? ? 2.407 ? ? 
metalc4  metalc ? ? G NA  .   NA ? ? ? 1_555 L HOH .   O  ? ? A NA  306 A HOH 521 1_555 ? ? ? ? ? ? ? 2.458 ? ? 
metalc5  metalc ? ? G NA  .   NA ? ? ? 1_555 L HOH .   O  ? ? A NA  306 A HOH 611 1_555 ? ? ? ? ? ? ? 2.425 ? ? 
metalc6  metalc ? ? G NA  .   NA ? ? ? 1_555 L HOH .   O  ? ? A NA  306 A HOH 629 1_555 ? ? ? ? ? ? ? 2.443 ? ? 
metalc7  metalc ? ? G NA  .   NA ? ? ? 1_555 L HOH .   O  ? ? A NA  306 A HOH 639 1_555 ? ? ? ? ? ? ? 2.411 ? ? 
metalc8  metalc ? ? G NA  .   NA ? ? ? 1_555 L HOH .   O  ? ? A NA  306 A HOH 661 1_555 ? ? ? ? ? ? ? 2.433 ? ? 
metalc9  metalc ? ? H NA  .   NA ? ? ? 1_555 L HOH .   O  ? ? A NA  307 A HOH 418 1_555 ? ? ? ? ? ? ? 2.363 ? ? 
metalc10 metalc ? ? H NA  .   NA ? ? ? 1_555 L HOH .   O  ? ? A NA  307 A HOH 628 4_455 ? ? ? ? ? ? ? 2.421 ? ? 
metalc11 metalc ? ? H NA  .   NA ? ? ? 1_555 L HOH .   O  ? ? A NA  307 A HOH 646 1_555 ? ? ? ? ? ? ? 2.424 ? ? 
metalc12 metalc ? ? H NA  .   NA ? ? ? 1_555 L HOH .   O  ? ? A NA  307 A HOH 667 4_455 ? ? ? ? ? ? ? 2.416 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OG ? A SER 79  ? A SER 79  ? 1_555 NA ? G NA . ? A NA 306 ? 1_555 O  ? L HOH .   ? A HOH 521 ? 1_555 103.7 ? 
2  OG ? A SER 79  ? A SER 79  ? 1_555 NA ? G NA . ? A NA 306 ? 1_555 O  ? L HOH .   ? A HOH 611 ? 1_555 84.8  ? 
3  O  ? L HOH .   ? A HOH 521 ? 1_555 NA ? G NA . ? A NA 306 ? 1_555 O  ? L HOH .   ? A HOH 611 ? 1_555 87.1  ? 
4  OG ? A SER 79  ? A SER 79  ? 1_555 NA ? G NA . ? A NA 306 ? 1_555 O  ? L HOH .   ? A HOH 629 ? 1_555 98.0  ? 
5  O  ? L HOH .   ? A HOH 521 ? 1_555 NA ? G NA . ? A NA 306 ? 1_555 O  ? L HOH .   ? A HOH 629 ? 1_555 95.1  ? 
6  O  ? L HOH .   ? A HOH 611 ? 1_555 NA ? G NA . ? A NA 306 ? 1_555 O  ? L HOH .   ? A HOH 629 ? 1_555 175.9 ? 
7  OG ? A SER 79  ? A SER 79  ? 1_555 NA ? G NA . ? A NA 306 ? 1_555 O  ? L HOH .   ? A HOH 639 ? 1_555 169.7 ? 
8  O  ? L HOH .   ? A HOH 521 ? 1_555 NA ? G NA . ? A NA 306 ? 1_555 O  ? L HOH .   ? A HOH 639 ? 1_555 86.5  ? 
9  O  ? L HOH .   ? A HOH 611 ? 1_555 NA ? G NA . ? A NA 306 ? 1_555 O  ? L HOH .   ? A HOH 639 ? 1_555 94.7  ? 
10 O  ? L HOH .   ? A HOH 629 ? 1_555 NA ? G NA . ? A NA 306 ? 1_555 O  ? L HOH .   ? A HOH 639 ? 1_555 82.0  ? 
11 OG ? A SER 79  ? A SER 79  ? 1_555 NA ? G NA . ? A NA 306 ? 1_555 O  ? L HOH .   ? A HOH 661 ? 1_555 90.2  ? 
12 O  ? L HOH .   ? A HOH 521 ? 1_555 NA ? G NA . ? A NA 306 ? 1_555 O  ? L HOH .   ? A HOH 661 ? 1_555 162.8 ? 
13 O  ? L HOH .   ? A HOH 611 ? 1_555 NA ? G NA . ? A NA 306 ? 1_555 O  ? L HOH .   ? A HOH 661 ? 1_555 84.2  ? 
14 O  ? L HOH .   ? A HOH 629 ? 1_555 NA ? G NA . ? A NA 306 ? 1_555 O  ? L HOH .   ? A HOH 661 ? 1_555 92.8  ? 
15 O  ? L HOH .   ? A HOH 639 ? 1_555 NA ? G NA . ? A NA 306 ? 1_555 O  ? L HOH .   ? A HOH 661 ? 1_555 79.5  ? 
16 O  ? A TYR 104 ? A TYR 104 ? 1_555 NA ? H NA . ? A NA 307 ? 4_565 OG ? A SER 141 ? A SER 141 ? 1_555 53.1  ? 
17 O  ? A TYR 104 ? A TYR 104 ? 1_555 NA ? H NA . ? A NA 307 ? 4_565 O  ? L HOH .   ? A HOH 418 ? 1_555 55.3  ? 
18 OG ? A SER 141 ? A SER 141 ? 1_555 NA ? H NA . ? A NA 307 ? 4_565 O  ? L HOH .   ? A HOH 418 ? 1_555 6.0   ? 
19 O  ? A TYR 104 ? A TYR 104 ? 1_555 NA ? H NA . ? A NA 307 ? 4_565 O  ? L HOH .   ? A HOH 628 ? 4_455 53.8  ? 
20 OG ? A SER 141 ? A SER 141 ? 1_555 NA ? H NA . ? A NA 307 ? 4_565 O  ? L HOH .   ? A HOH 628 ? 4_455 4.5   ? 
21 O  ? L HOH .   ? A HOH 418 ? 1_555 NA ? H NA . ? A NA 307 ? 4_565 O  ? L HOH .   ? A HOH 628 ? 4_455 1.9   ? 
22 O  ? A TYR 104 ? A TYR 104 ? 1_555 NA ? H NA . ? A NA 307 ? 4_565 O  ? L HOH .   ? A HOH 646 ? 1_555 49.6  ? 
23 OG ? A SER 141 ? A SER 141 ? 1_555 NA ? H NA . ? A NA 307 ? 4_565 O  ? L HOH .   ? A HOH 646 ? 1_555 5.2   ? 
24 O  ? L HOH .   ? A HOH 418 ? 1_555 NA ? H NA . ? A NA 307 ? 4_565 O  ? L HOH .   ? A HOH 646 ? 1_555 5.9   ? 
25 O  ? L HOH .   ? A HOH 628 ? 4_455 NA ? H NA . ? A NA 307 ? 4_565 O  ? L HOH .   ? A HOH 646 ? 1_555 4.2   ? 
26 O  ? A TYR 104 ? A TYR 104 ? 1_555 NA ? H NA . ? A NA 307 ? 4_565 O  ? L HOH .   ? A HOH 667 ? 4_455 51.8  ? 
27 OG ? A SER 141 ? A SER 141 ? 1_555 NA ? H NA . ? A NA 307 ? 4_565 O  ? L HOH .   ? A HOH 667 ? 4_455 1.3   ? 
28 O  ? L HOH .   ? A HOH 418 ? 1_555 NA ? H NA . ? A NA 307 ? 4_565 O  ? L HOH .   ? A HOH 667 ? 4_455 6.5   ? 
29 O  ? L HOH .   ? A HOH 628 ? 4_455 NA ? H NA . ? A NA 307 ? 4_565 O  ? L HOH .   ? A HOH 667 ? 4_455 4.8   ? 
30 O  ? L HOH .   ? A HOH 646 ? 1_555 NA ? H NA . ? A NA 307 ? 4_565 O  ? L HOH .   ? A HOH 667 ? 4_455 4.3   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 24  ? CYS A 98  ? CYS A 24  ? 1_555 CYS A 98  ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 157 ? CYS A 226 ? CYS A 157 ? 1_555 CYS A 226 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 141 A . ? SER 141 A PRO 142 A ? PRO 142 A 1 -6.94 
2 HIS 214 A . ? HIS 214 A PRO 215 A ? PRO 215 A 1 -6.30 
3 ASP 232 A . ? ASP 232 A PRO 233 A ? PRO 233 A 1 -5.02 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 6 ? 
AA3 ? 4 ? 
AA4 ? 4 ? 
AA5 ? 6 ? 
AA6 ? 4 ? 
AA7 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLN A 5   ? GLN A 7   ? GLN A 5   GLN A 7   
AA1 2 VAL A 20  ? SER A 27  ? VAL A 20  SER A 27  
AA1 3 THR A 80  ? LEU A 85  ? THR A 80  LEU A 85  
AA1 4 ALA A 70  ? ASP A 75  ? ALA A 70  ASP A 75  
AA2 1 THR A 11  ? VAL A 14  ? THR A 11  VAL A 14  
AA2 2 THR A 112 ? VAL A 116 ? THR A 112 VAL A 116 
AA2 3 ALA A 94  ? ARG A 100 ? ALA A 94  ARG A 100 
AA2 4 LEU A 36  ? THR A 42  ? LEU A 36  THR A 42  
AA2 5 GLY A 46  ? ILE A 53  ? GLY A 46  ILE A 53  
AA2 6 THR A 60  ? TYR A 62  ? THR A 60  TYR A 62  
AA3 1 THR A 11  ? VAL A 14  ? THR A 11  VAL A 14  
AA3 2 THR A 112 ? VAL A 116 ? THR A 112 VAL A 116 
AA3 3 ALA A 94  ? ARG A 100 ? ALA A 94  ARG A 100 
AA3 4 LEU A 107 ? TRP A 108 ? LEU A 107 TRP A 108 
AA4 1 LEU A 138 ? SER A 141 ? LEU A 138 SER A 141 
AA4 2 ALA A 153 ? ALA A 159 ? ALA A 153 ALA A 159 
AA4 3 ASP A 208 ? ILE A 213 ? ASP A 208 ILE A 213 
AA4 4 PHE A 200 ? SER A 205 ? PHE A 200 SER A 205 
AA5 1 SER A 144 ? VAL A 147 ? SER A 144 VAL A 147 
AA5 2 THR A 240 ? ILE A 244 ? THR A 240 ILE A 244 
AA5 3 ALA A 222 ? GLN A 228 ? ALA A 222 GLN A 228 
AA5 4 MET A 171 ? GLN A 176 ? MET A 171 GLN A 176 
AA5 5 ARG A 183 ? TYR A 187 ? ARG A 183 TYR A 187 
AA5 6 ASN A 191 ? LEU A 192 ? ASN A 191 LEU A 192 
AA6 1 SER A 144 ? VAL A 147 ? SER A 144 VAL A 147 
AA6 2 THR A 240 ? ILE A 244 ? THR A 240 ILE A 244 
AA6 3 ALA A 222 ? GLN A 228 ? ALA A 222 GLN A 228 
AA6 4 THR A 235 ? PHE A 236 ? THR A 235 PHE A 236 
AA7 1 ASP A 164 ? TYR A 165 ? ASP A 164 TYR A 165 
AA7 2 ASP A 168 ? SER A 169 ? ASP A 168 SER A 169 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N GLN A 7   ? N GLN A 7   O LYS A 25  ? O LYS A 25  
AA1 2 3 N LEU A 22  ? N LEU A 22  O MET A 83  ? O MET A 83  
AA1 3 4 O THR A 80  ? O THR A 80  N ASP A 75  ? N ASP A 75  
AA2 1 2 N GLU A 12  ? N GLU A 12  O THR A 113 ? O THR A 113 
AA2 2 3 O VAL A 114 ? O VAL A 114 N ALA A 94  ? N ALA A 94  
AA2 3 4 O VAL A 95  ? O VAL A 95  N GLN A 41  ? N GLN A 41  
AA2 4 5 N LEU A 36  ? N LEU A 36  O ILE A 53  ? O ILE A 53  
AA2 5 6 N ALA A 52  ? N ALA A 52  O SER A 61  ? O SER A 61  
AA3 1 2 N GLU A 12  ? N GLU A 12  O THR A 113 ? O THR A 113 
AA3 2 3 O VAL A 114 ? O VAL A 114 N ALA A 94  ? N ALA A 94  
AA3 3 4 N ARG A 100 ? N ARG A 100 O LEU A 107 ? O LEU A 107 
AA4 1 2 N SER A 141 ? N SER A 141 O SER A 156 ? O SER A 156 
AA4 2 3 N ILE A 155 ? N ILE A 155 O LEU A 211 ? O LEU A 211 
AA4 3 4 O ASN A 212 ? O ASN A 212 N SER A 201 ? N SER A 201 
AA5 1 2 N LEU A 145 ? N LEU A 145 O GLU A 243 ? O GLU A 243 
AA5 2 3 O LEU A 242 ? O LEU A 242 N ALA A 222 ? N ALA A 222 
AA5 3 4 O TYR A 225 ? O TYR A 225 N TYR A 174 ? N TYR A 174 
AA5 4 5 N TRP A 173 ? N TRP A 173 O LEU A 185 ? O LEU A 185 
AA5 5 6 N TYR A 187 ? N TYR A 187 O ASN A 191 ? O ASN A 191 
AA6 1 2 N LEU A 145 ? N LEU A 145 O GLU A 243 ? O GLU A 243 
AA6 2 3 O LEU A 242 ? O LEU A 242 N ALA A 222 ? N ALA A 222 
AA6 3 4 N GLN A 228 ? N GLN A 228 O THR A 235 ? O THR A 235 
AA7 1 2 N TYR A 165 ? N TYR A 165 O ASP A 168 ? O ASP A 168 
# 
_pdbx_entry_details.entry_id                   9HY3 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ALA A 94  ? ? 177.39 169.38 
2 1 ALA A 189 ? ? 72.86  -39.22 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     510 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   L 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         -32.0052 
_pdbx_refine_tls.origin_y         6.2983 
_pdbx_refine_tls.origin_z         9.7419 
_pdbx_refine_tls.T[1][1]          0.1432 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0458 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0475 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.0584 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0309 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.0870 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.1220 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.0288 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.0145 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.3886 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.0343 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.5324 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0233 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.0157 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0453 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0225 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.1210 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0512 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.0717 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0233 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0977 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     3 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    A 
_pdbx_refine_tls_group.end_auth_seq_id     304 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   ? 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 732 ? 5.82 . 
2 1 O ? A HOH 733 ? 6.25 . 
3 1 O ? A HOH 734 ? 7.26 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A ASP 2   ? A ASP 2   
3  1 Y 1 A GLY 121 ? A GLY 121 
4  1 Y 1 A GLY 122 ? A GLY 122 
5  1 Y 1 A GLY 123 ? A GLY 123 
6  1 Y 1 A SER 124 ? A SER 124 
7  1 Y 1 A GLY 125 ? A GLY 125 
8  1 Y 1 A GLY 126 ? A GLY 126 
9  1 Y 1 A GLY 127 ? A GLY 127 
10 1 Y 1 A GLY 128 ? A GLY 128 
11 1 Y 1 A SER 129 ? A SER 129 
12 1 Y 1 A GLY 130 ? A GLY 130 
13 1 Y 1 A GLY 131 ? A GLY 131 
14 1 Y 1 A GLY 132 ? A GLY 132 
15 1 Y 1 A GLY 133 ? A GLY 133 
16 1 Y 1 A MET 248 ? A MET 248 
17 1 Y 1 A GLY 249 ? A GLY 249 
18 1 Y 1 A SER 250 ? A SER 250 
19 1 Y 1 A SER 251 ? A SER 251 
20 1 Y 1 A HIS 252 ? A HIS 252 
21 1 Y 1 A HIS 253 ? A HIS 253 
22 1 Y 1 A HIS 254 ? A HIS 254 
23 1 Y 1 A HIS 255 ? A HIS 255 
24 1 Y 1 A HIS 256 ? A HIS 256 
25 1 Y 1 A HIS 257 ? A HIS 257 
26 1 Y 1 A SER 258 ? A SER 258 
27 1 Y 1 A SER 259 ? A SER 259 
28 1 Y 1 A GLY 260 ? A GLY 260 
29 1 Y 1 A GLU 261 ? A GLU 261 
30 1 Y 1 A ASN 262 ? A ASN 262 
31 1 Y 1 A LEU 263 ? A LEU 263 
32 1 Y 1 A TYR 264 ? A TYR 264 
33 1 Y 1 A PHE 265 ? A PHE 265 
34 1 Y 1 A GLN 266 ? A GLN 266 
35 1 Y 1 A GLY 267 ? A GLY 267 
36 1 Y 1 A HIS 268 ? A HIS 268 
37 1 Y 1 A MET 269 ? A MET 269 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CL  CL   CL N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
EDO C1   C  N N 89  
EDO O1   O  N N 90  
EDO C2   C  N N 91  
EDO O2   O  N N 92  
EDO H11  H  N N 93  
EDO H12  H  N N 94  
EDO HO1  H  N N 95  
EDO H21  H  N N 96  
EDO H22  H  N N 97  
EDO HO2  H  N N 98  
GLN N    N  N N 99  
GLN CA   C  N S 100 
GLN C    C  N N 101 
GLN O    O  N N 102 
GLN CB   C  N N 103 
GLN CG   C  N N 104 
GLN CD   C  N N 105 
GLN OE1  O  N N 106 
GLN NE2  N  N N 107 
GLN OXT  O  N N 108 
GLN H    H  N N 109 
GLN H2   H  N N 110 
GLN HA   H  N N 111 
GLN HB2  H  N N 112 
GLN HB3  H  N N 113 
GLN HG2  H  N N 114 
GLN HG3  H  N N 115 
GLN HE21 H  N N 116 
GLN HE22 H  N N 117 
GLN HXT  H  N N 118 
GLU N    N  N N 119 
GLU CA   C  N S 120 
GLU C    C  N N 121 
GLU O    O  N N 122 
GLU CB   C  N N 123 
GLU CG   C  N N 124 
GLU CD   C  N N 125 
GLU OE1  O  N N 126 
GLU OE2  O  N N 127 
GLU OXT  O  N N 128 
GLU H    H  N N 129 
GLU H2   H  N N 130 
GLU HA   H  N N 131 
GLU HB2  H  N N 132 
GLU HB3  H  N N 133 
GLU HG2  H  N N 134 
GLU HG3  H  N N 135 
GLU HE2  H  N N 136 
GLU HXT  H  N N 137 
GLY N    N  N N 138 
GLY CA   C  N N 139 
GLY C    C  N N 140 
GLY O    O  N N 141 
GLY OXT  O  N N 142 
GLY H    H  N N 143 
GLY H2   H  N N 144 
GLY HA2  H  N N 145 
GLY HA3  H  N N 146 
GLY HXT  H  N N 147 
HIS N    N  N N 148 
HIS CA   C  N S 149 
HIS C    C  N N 150 
HIS O    O  N N 151 
HIS CB   C  N N 152 
HIS CG   C  Y N 153 
HIS ND1  N  Y N 154 
HIS CD2  C  Y N 155 
HIS CE1  C  Y N 156 
HIS NE2  N  Y N 157 
HIS OXT  O  N N 158 
HIS H    H  N N 159 
HIS H2   H  N N 160 
HIS HA   H  N N 161 
HIS HB2  H  N N 162 
HIS HB3  H  N N 163 
HIS HD1  H  N N 164 
HIS HD2  H  N N 165 
HIS HE1  H  N N 166 
HIS HE2  H  N N 167 
HIS HXT  H  N N 168 
HOH O    O  N N 169 
HOH H1   H  N N 170 
HOH H2   H  N N 171 
ILE N    N  N N 172 
ILE CA   C  N S 173 
ILE C    C  N N 174 
ILE O    O  N N 175 
ILE CB   C  N S 176 
ILE CG1  C  N N 177 
ILE CG2  C  N N 178 
ILE CD1  C  N N 179 
ILE OXT  O  N N 180 
ILE H    H  N N 181 
ILE H2   H  N N 182 
ILE HA   H  N N 183 
ILE HB   H  N N 184 
ILE HG12 H  N N 185 
ILE HG13 H  N N 186 
ILE HG21 H  N N 187 
ILE HG22 H  N N 188 
ILE HG23 H  N N 189 
ILE HD11 H  N N 190 
ILE HD12 H  N N 191 
ILE HD13 H  N N 192 
ILE HXT  H  N N 193 
IMD N1   N  Y N 194 
IMD C2   C  Y N 195 
IMD N3   N  Y N 196 
IMD C4   C  Y N 197 
IMD C5   C  Y N 198 
IMD HN1  H  N N 199 
IMD H2   H  N N 200 
IMD HN3  H  N N 201 
IMD H4   H  N N 202 
IMD H5   H  N N 203 
LEU N    N  N N 204 
LEU CA   C  N S 205 
LEU C    C  N N 206 
LEU O    O  N N 207 
LEU CB   C  N N 208 
LEU CG   C  N N 209 
LEU CD1  C  N N 210 
LEU CD2  C  N N 211 
LEU OXT  O  N N 212 
LEU H    H  N N 213 
LEU H2   H  N N 214 
LEU HA   H  N N 215 
LEU HB2  H  N N 216 
LEU HB3  H  N N 217 
LEU HG   H  N N 218 
LEU HD11 H  N N 219 
LEU HD12 H  N N 220 
LEU HD13 H  N N 221 
LEU HD21 H  N N 222 
LEU HD22 H  N N 223 
LEU HD23 H  N N 224 
LEU HXT  H  N N 225 
LYS N    N  N N 226 
LYS CA   C  N S 227 
LYS C    C  N N 228 
LYS O    O  N N 229 
LYS CB   C  N N 230 
LYS CG   C  N N 231 
LYS CD   C  N N 232 
LYS CE   C  N N 233 
LYS NZ   N  N N 234 
LYS OXT  O  N N 235 
LYS H    H  N N 236 
LYS H2   H  N N 237 
LYS HA   H  N N 238 
LYS HB2  H  N N 239 
LYS HB3  H  N N 240 
LYS HG2  H  N N 241 
LYS HG3  H  N N 242 
LYS HD2  H  N N 243 
LYS HD3  H  N N 244 
LYS HE2  H  N N 245 
LYS HE3  H  N N 246 
LYS HZ1  H  N N 247 
LYS HZ2  H  N N 248 
LYS HZ3  H  N N 249 
LYS HXT  H  N N 250 
MET N    N  N N 251 
MET CA   C  N S 252 
MET C    C  N N 253 
MET O    O  N N 254 
MET CB   C  N N 255 
MET CG   C  N N 256 
MET SD   S  N N 257 
MET CE   C  N N 258 
MET OXT  O  N N 259 
MET H    H  N N 260 
MET H2   H  N N 261 
MET HA   H  N N 262 
MET HB2  H  N N 263 
MET HB3  H  N N 264 
MET HG2  H  N N 265 
MET HG3  H  N N 266 
MET HE1  H  N N 267 
MET HE2  H  N N 268 
MET HE3  H  N N 269 
MET HXT  H  N N 270 
NA  NA   NA N N 271 
PHE N    N  N N 272 
PHE CA   C  N S 273 
PHE C    C  N N 274 
PHE O    O  N N 275 
PHE CB   C  N N 276 
PHE CG   C  Y N 277 
PHE CD1  C  Y N 278 
PHE CD2  C  Y N 279 
PHE CE1  C  Y N 280 
PHE CE2  C  Y N 281 
PHE CZ   C  Y N 282 
PHE OXT  O  N N 283 
PHE H    H  N N 284 
PHE H2   H  N N 285 
PHE HA   H  N N 286 
PHE HB2  H  N N 287 
PHE HB3  H  N N 288 
PHE HD1  H  N N 289 
PHE HD2  H  N N 290 
PHE HE1  H  N N 291 
PHE HE2  H  N N 292 
PHE HZ   H  N N 293 
PHE HXT  H  N N 294 
PRO N    N  N N 295 
PRO CA   C  N S 296 
PRO C    C  N N 297 
PRO O    O  N N 298 
PRO CB   C  N N 299 
PRO CG   C  N N 300 
PRO CD   C  N N 301 
PRO OXT  O  N N 302 
PRO H    H  N N 303 
PRO HA   H  N N 304 
PRO HB2  H  N N 305 
PRO HB3  H  N N 306 
PRO HG2  H  N N 307 
PRO HG3  H  N N 308 
PRO HD2  H  N N 309 
PRO HD3  H  N N 310 
PRO HXT  H  N N 311 
SER N    N  N N 312 
SER CA   C  N S 313 
SER C    C  N N 314 
SER O    O  N N 315 
SER CB   C  N N 316 
SER OG   O  N N 317 
SER OXT  O  N N 318 
SER H    H  N N 319 
SER H2   H  N N 320 
SER HA   H  N N 321 
SER HB2  H  N N 322 
SER HB3  H  N N 323 
SER HG   H  N N 324 
SER HXT  H  N N 325 
THR N    N  N N 326 
THR CA   C  N S 327 
THR C    C  N N 328 
THR O    O  N N 329 
THR CB   C  N R 330 
THR OG1  O  N N 331 
THR CG2  C  N N 332 
THR OXT  O  N N 333 
THR H    H  N N 334 
THR H2   H  N N 335 
THR HA   H  N N 336 
THR HB   H  N N 337 
THR HG1  H  N N 338 
THR HG21 H  N N 339 
THR HG22 H  N N 340 
THR HG23 H  N N 341 
THR HXT  H  N N 342 
TRP N    N  N N 343 
TRP CA   C  N S 344 
TRP C    C  N N 345 
TRP O    O  N N 346 
TRP CB   C  N N 347 
TRP CG   C  Y N 348 
TRP CD1  C  Y N 349 
TRP CD2  C  Y N 350 
TRP NE1  N  Y N 351 
TRP CE2  C  Y N 352 
TRP CE3  C  Y N 353 
TRP CZ2  C  Y N 354 
TRP CZ3  C  Y N 355 
TRP CH2  C  Y N 356 
TRP OXT  O  N N 357 
TRP H    H  N N 358 
TRP H2   H  N N 359 
TRP HA   H  N N 360 
TRP HB2  H  N N 361 
TRP HB3  H  N N 362 
TRP HD1  H  N N 363 
TRP HE1  H  N N 364 
TRP HE3  H  N N 365 
TRP HZ2  H  N N 366 
TRP HZ3  H  N N 367 
TRP HH2  H  N N 368 
TRP HXT  H  N N 369 
TYR N    N  N N 370 
TYR CA   C  N S 371 
TYR C    C  N N 372 
TYR O    O  N N 373 
TYR CB   C  N N 374 
TYR CG   C  Y N 375 
TYR CD1  C  Y N 376 
TYR CD2  C  Y N 377 
TYR CE1  C  Y N 378 
TYR CE2  C  Y N 379 
TYR CZ   C  Y N 380 
TYR OH   O  N N 381 
TYR OXT  O  N N 382 
TYR H    H  N N 383 
TYR H2   H  N N 384 
TYR HA   H  N N 385 
TYR HB2  H  N N 386 
TYR HB3  H  N N 387 
TYR HD1  H  N N 388 
TYR HD2  H  N N 389 
TYR HE1  H  N N 390 
TYR HE2  H  N N 391 
TYR HH   H  N N 392 
TYR HXT  H  N N 393 
VAL N    N  N N 394 
VAL CA   C  N S 395 
VAL C    C  N N 396 
VAL O    O  N N 397 
VAL CB   C  N N 398 
VAL CG1  C  N N 399 
VAL CG2  C  N N 400 
VAL OXT  O  N N 401 
VAL H    H  N N 402 
VAL H2   H  N N 403 
VAL HA   H  N N 404 
VAL HB   H  N N 405 
VAL HG11 H  N N 406 
VAL HG12 H  N N 407 
VAL HG13 H  N N 408 
VAL HG21 H  N N 409 
VAL HG22 H  N N 410 
VAL HG23 H  N N 411 
VAL HXT  H  N N 412 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
IMD N1  C2   sing Y N 182 
IMD N1  C5   sing Y N 183 
IMD N1  HN1  sing N N 184 
IMD C2  N3   doub Y N 185 
IMD C2  H2   sing N N 186 
IMD N3  C4   sing Y N 187 
IMD N3  HN3  sing N N 188 
IMD C4  C5   doub Y N 189 
IMD C4  H4   sing N N 190 
IMD C5  H5   sing N N 191 
LEU N   CA   sing N N 192 
LEU N   H    sing N N 193 
LEU N   H2   sing N N 194 
LEU CA  C    sing N N 195 
LEU CA  CB   sing N N 196 
LEU CA  HA   sing N N 197 
LEU C   O    doub N N 198 
LEU C   OXT  sing N N 199 
LEU CB  CG   sing N N 200 
LEU CB  HB2  sing N N 201 
LEU CB  HB3  sing N N 202 
LEU CG  CD1  sing N N 203 
LEU CG  CD2  sing N N 204 
LEU CG  HG   sing N N 205 
LEU CD1 HD11 sing N N 206 
LEU CD1 HD12 sing N N 207 
LEU CD1 HD13 sing N N 208 
LEU CD2 HD21 sing N N 209 
LEU CD2 HD22 sing N N 210 
LEU CD2 HD23 sing N N 211 
LEU OXT HXT  sing N N 212 
LYS N   CA   sing N N 213 
LYS N   H    sing N N 214 
LYS N   H2   sing N N 215 
LYS CA  C    sing N N 216 
LYS CA  CB   sing N N 217 
LYS CA  HA   sing N N 218 
LYS C   O    doub N N 219 
LYS C   OXT  sing N N 220 
LYS CB  CG   sing N N 221 
LYS CB  HB2  sing N N 222 
LYS CB  HB3  sing N N 223 
LYS CG  CD   sing N N 224 
LYS CG  HG2  sing N N 225 
LYS CG  HG3  sing N N 226 
LYS CD  CE   sing N N 227 
LYS CD  HD2  sing N N 228 
LYS CD  HD3  sing N N 229 
LYS CE  NZ   sing N N 230 
LYS CE  HE2  sing N N 231 
LYS CE  HE3  sing N N 232 
LYS NZ  HZ1  sing N N 233 
LYS NZ  HZ2  sing N N 234 
LYS NZ  HZ3  sing N N 235 
LYS OXT HXT  sing N N 236 
MET N   CA   sing N N 237 
MET N   H    sing N N 238 
MET N   H2   sing N N 239 
MET CA  C    sing N N 240 
MET CA  CB   sing N N 241 
MET CA  HA   sing N N 242 
MET C   O    doub N N 243 
MET C   OXT  sing N N 244 
MET CB  CG   sing N N 245 
MET CB  HB2  sing N N 246 
MET CB  HB3  sing N N 247 
MET CG  SD   sing N N 248 
MET CG  HG2  sing N N 249 
MET CG  HG3  sing N N 250 
MET SD  CE   sing N N 251 
MET CE  HE1  sing N N 252 
MET CE  HE2  sing N N 253 
MET CE  HE3  sing N N 254 
MET OXT HXT  sing N N 255 
PHE N   CA   sing N N 256 
PHE N   H    sing N N 257 
PHE N   H2   sing N N 258 
PHE CA  C    sing N N 259 
PHE CA  CB   sing N N 260 
PHE CA  HA   sing N N 261 
PHE C   O    doub N N 262 
PHE C   OXT  sing N N 263 
PHE CB  CG   sing N N 264 
PHE CB  HB2  sing N N 265 
PHE CB  HB3  sing N N 266 
PHE CG  CD1  doub Y N 267 
PHE CG  CD2  sing Y N 268 
PHE CD1 CE1  sing Y N 269 
PHE CD1 HD1  sing N N 270 
PHE CD2 CE2  doub Y N 271 
PHE CD2 HD2  sing N N 272 
PHE CE1 CZ   doub Y N 273 
PHE CE1 HE1  sing N N 274 
PHE CE2 CZ   sing Y N 275 
PHE CE2 HE2  sing N N 276 
PHE CZ  HZ   sing N N 277 
PHE OXT HXT  sing N N 278 
PRO N   CA   sing N N 279 
PRO N   CD   sing N N 280 
PRO N   H    sing N N 281 
PRO CA  C    sing N N 282 
PRO CA  CB   sing N N 283 
PRO CA  HA   sing N N 284 
PRO C   O    doub N N 285 
PRO C   OXT  sing N N 286 
PRO CB  CG   sing N N 287 
PRO CB  HB2  sing N N 288 
PRO CB  HB3  sing N N 289 
PRO CG  CD   sing N N 290 
PRO CG  HG2  sing N N 291 
PRO CG  HG3  sing N N 292 
PRO CD  HD2  sing N N 293 
PRO CD  HD3  sing N N 294 
PRO OXT HXT  sing N N 295 
SER N   CA   sing N N 296 
SER N   H    sing N N 297 
SER N   H2   sing N N 298 
SER CA  C    sing N N 299 
SER CA  CB   sing N N 300 
SER CA  HA   sing N N 301 
SER C   O    doub N N 302 
SER C   OXT  sing N N 303 
SER CB  OG   sing N N 304 
SER CB  HB2  sing N N 305 
SER CB  HB3  sing N N 306 
SER OG  HG   sing N N 307 
SER OXT HXT  sing N N 308 
THR N   CA   sing N N 309 
THR N   H    sing N N 310 
THR N   H2   sing N N 311 
THR CA  C    sing N N 312 
THR CA  CB   sing N N 313 
THR CA  HA   sing N N 314 
THR C   O    doub N N 315 
THR C   OXT  sing N N 316 
THR CB  OG1  sing N N 317 
THR CB  CG2  sing N N 318 
THR CB  HB   sing N N 319 
THR OG1 HG1  sing N N 320 
THR CG2 HG21 sing N N 321 
THR CG2 HG22 sing N N 322 
THR CG2 HG23 sing N N 323 
THR OXT HXT  sing N N 324 
TRP N   CA   sing N N 325 
TRP N   H    sing N N 326 
TRP N   H2   sing N N 327 
TRP CA  C    sing N N 328 
TRP CA  CB   sing N N 329 
TRP CA  HA   sing N N 330 
TRP C   O    doub N N 331 
TRP C   OXT  sing N N 332 
TRP CB  CG   sing N N 333 
TRP CB  HB2  sing N N 334 
TRP CB  HB3  sing N N 335 
TRP CG  CD1  doub Y N 336 
TRP CG  CD2  sing Y N 337 
TRP CD1 NE1  sing Y N 338 
TRP CD1 HD1  sing N N 339 
TRP CD2 CE2  doub Y N 340 
TRP CD2 CE3  sing Y N 341 
TRP NE1 CE2  sing Y N 342 
TRP NE1 HE1  sing N N 343 
TRP CE2 CZ2  sing Y N 344 
TRP CE3 CZ3  doub Y N 345 
TRP CE3 HE3  sing N N 346 
TRP CZ2 CH2  doub Y N 347 
TRP CZ2 HZ2  sing N N 348 
TRP CZ3 CH2  sing Y N 349 
TRP CZ3 HZ3  sing N N 350 
TRP CH2 HH2  sing N N 351 
TRP OXT HXT  sing N N 352 
TYR N   CA   sing N N 353 
TYR N   H    sing N N 354 
TYR N   H2   sing N N 355 
TYR CA  C    sing N N 356 
TYR CA  CB   sing N N 357 
TYR CA  HA   sing N N 358 
TYR C   O    doub N N 359 
TYR C   OXT  sing N N 360 
TYR CB  CG   sing N N 361 
TYR CB  HB2  sing N N 362 
TYR CB  HB3  sing N N 363 
TYR CG  CD1  doub Y N 364 
TYR CG  CD2  sing Y N 365 
TYR CD1 CE1  sing Y N 366 
TYR CD1 HD1  sing N N 367 
TYR CD2 CE2  doub Y N 368 
TYR CD2 HD2  sing N N 369 
TYR CE1 CZ   doub Y N 370 
TYR CE1 HE1  sing N N 371 
TYR CE2 CZ   sing Y N 372 
TYR CE2 HE2  sing N N 373 
TYR CZ  OH   sing N N 374 
TYR OH  HH   sing N N 375 
TYR OXT HXT  sing N N 376 
VAL N   CA   sing N N 377 
VAL N   H    sing N N 378 
VAL N   H2   sing N N 379 
VAL CA  C    sing N N 380 
VAL CA  CB   sing N N 381 
VAL CA  HA   sing N N 382 
VAL C   O    doub N N 383 
VAL C   OXT  sing N N 384 
VAL CB  CG1  sing N N 385 
VAL CB  CG2  sing N N 386 
VAL CB  HB   sing N N 387 
VAL CG1 HG11 sing N N 388 
VAL CG1 HG12 sing N N 389 
VAL CG1 HG13 sing N N 390 
VAL CG2 HG21 sing N N 391 
VAL CG2 HG22 sing N N 392 
VAL CG2 HG23 sing N N 393 
VAL OXT HXT  sing N N 394 
# 
_pdbx_audit_support.funding_organization   'European Union (EU)' 
_pdbx_audit_support.country                'European Union' 
_pdbx_audit_support.grant_number           BC63C22000680007 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7DET 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9HY3 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.015496 
_atom_sites.fract_transf_matrix[1][2]   0.008947 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017894 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.006230 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
NA 
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . GLN A 1 3   ? -11.918 12.874  14.902  1.00 57.17 ? 3   GLN A N   1 
ATOM   2    C  CA  . GLN A 1 3   ? -12.974 12.337  13.997  1.00 54.47 ? 3   GLN A CA  1 
ATOM   3    C  C   . GLN A 1 3   ? -14.334 12.900  14.420  1.00 47.61 ? 3   GLN A C   1 
ATOM   4    O  O   . GLN A 1 3   ? -14.549 13.255  15.578  1.00 53.36 ? 3   GLN A O   1 
ATOM   5    C  CB  . GLN A 1 3   ? -12.975 10.806  13.964  1.00 61.10 ? 3   GLN A CB  1 
ATOM   6    N  N   . GLU A 1 4   ? -15.260 12.971  13.466  1.00 43.72 ? 4   GLU A N   1 
ATOM   7    C  CA  . GLU A 1 4   ? -16.585 13.493  13.754  1.00 39.78 ? 4   GLU A CA  1 
ATOM   8    C  C   . GLU A 1 4   ? -17.392 12.457  14.530  1.00 37.97 ? 4   GLU A C   1 
ATOM   9    O  O   . GLU A 1 4   ? -17.431 11.289  14.126  1.00 37.17 ? 4   GLU A O   1 
ATOM   10   C  CB  . GLU A 1 4   ? -17.174 13.783  12.389  1.00 40.26 ? 4   GLU A CB  1 
ATOM   11   C  CG  . GLU A 1 4   ? -16.247 14.710  11.613  1.00 46.92 ? 4   GLU A CG  1 
ATOM   12   C  CD  . GLU A 1 4   ? -16.807 15.149  10.289  1.00 48.82 ? 4   GLU A CD  1 
ATOM   13   O  OE1 . GLU A 1 4   ? -17.976 15.557  10.278  1.00 48.55 ? 4   GLU A OE1 1 
ATOM   14   O  OE2 . GLU A 1 4   ? -16.069 15.155  9.285   1.00 61.43 ? 4   GLU A OE2 1 
ATOM   15   N  N   . GLN A 1 5   ? -18.026 12.897  15.625  1.00 33.86 ? 5   GLN A N   1 
ATOM   16   C  CA  . GLN A 1 5   ? -18.786 11.964  16.419  1.00 34.81 ? 5   GLN A CA  1 
ATOM   17   C  C   . GLN A 1 5   ? -20.060 12.647  16.856  1.00 29.61 ? 5   GLN A C   1 
ATOM   18   O  O   . GLN A 1 5   ? -20.074 13.836  17.108  1.00 28.47 ? 5   GLN A O   1 
ATOM   19   C  CB  . GLN A 1 5   ? -18.104 11.711  17.753  1.00 40.20 ? 5   GLN A CB  1 
ATOM   20   C  CG  . GLN A 1 5   ? -16.726 11.082  17.661  0.70 45.51 ? 5   GLN A CG  1 
ATOM   21   C  CD  . GLN A 1 5   ? -16.265 10.729  19.054  0.70 49.70 ? 5   GLN A CD  1 
ATOM   22   O  OE1 . GLN A 1 5   ? -16.807 9.816   19.681  0.70 55.51 ? 5   GLN A OE1 1 
ATOM   23   N  NE2 . GLN A 1 5   ? -15.341 11.515  19.589  0.70 53.82 ? 5   GLN A NE2 1 
ATOM   24   N  N   . LEU A 1 6   ? -21.098 11.836  17.027  1.00 28.21 ? 6   LEU A N   1 
ATOM   25   C  CA  . LEU A 1 6   ? -22.291 12.283  17.709  1.00 26.93 ? 6   LEU A CA  1 
ATOM   26   C  C   . LEU A 1 6   ? -22.475 11.299  18.868  1.00 29.28 ? 6   LEU A C   1 
ATOM   27   O  O   . LEU A 1 6   ? -22.693 10.108  18.608  1.00 30.93 ? 6   LEU A O   1 
ATOM   28   C  CB  . LEU A 1 6   ? -23.481 12.135  16.759  1.00 27.61 ? 6   LEU A CB  1 
ATOM   29   C  CG  . LEU A 1 6   ? -23.371 12.891  15.422  1.00 28.18 ? 6   LEU A CG  1 
ATOM   30   C  CD1 . LEU A 1 6   ? -24.583 12.594  14.471  1.00 24.56 ? 6   LEU A CD1 1 
ATOM   31   C  CD2 . LEU A 1 6   ? -23.269 14.382  15.780  1.00 28.00 ? 6   LEU A CD2 1 
ATOM   32   N  N   . GLN A 1 7   ? -22.409 11.787  20.098  1.00 28.09 ? 7   GLN A N   1 
ATOM   33   C  CA  . GLN A 1 7   ? -22.379 10.899  21.264  1.00 28.46 ? 7   GLN A CA  1 
ATOM   34   C  C   . GLN A 1 7   ? -23.711 11.016  22.012  1.00 28.24 ? 7   GLN A C   1 
ATOM   35   O  O   . GLN A 1 7   ? -24.098 12.108  22.473  1.00 27.88 ? 7   GLN A O   1 
ATOM   36   C  CB  . GLN A 1 7   ? -21.196 11.290  22.156  1.00 32.64 ? 7   GLN A CB  1 
ATOM   37   C  CG  . GLN A 1 7   ? -21.241 10.629  23.534  1.00 41.52 ? 7   GLN A CG  1 
ATOM   38   C  CD  . GLN A 1 7   ? -20.044 11.011  24.379  0.70 44.61 ? 7   GLN A CD  1 
ATOM   39   O  OE1 . GLN A 1 7   ? -18.887 10.751  24.018  0.70 48.53 ? 7   GLN A OE1 1 
ATOM   40   N  NE2 . GLN A 1 7   ? -20.317 11.669  25.492  0.70 49.26 ? 7   GLN A NE2 1 
ATOM   41   N  N   . GLN A 1 8   ? -24.412 9.881   22.151  1.00 24.76 ? 8   GLN A N   1 
ATOM   42   C  CA  . GLN A 1 8   ? -25.694 9.806   22.828  1.00 25.69 ? 8   GLN A CA  1 
ATOM   43   C  C   . GLN A 1 8   ? -25.622 8.816   24.013  1.00 27.56 ? 8   GLN A C   1 
ATOM   44   O  O   . GLN A 1 8   ? -25.054 7.724   23.845  1.00 28.49 ? 8   GLN A O   1 
ATOM   45   C  CB  . GLN A 1 8   ? -26.721 9.200   21.869  1.00 26.03 ? 8   GLN A CB  1 
ATOM   46   C  CG  . GLN A 1 8   ? -27.001 10.106  20.655  1.00 25.99 ? 8   GLN A CG  1 
ATOM   47   C  CD  . GLN A 1 8   ? -28.105 9.556   19.768  1.00 26.60 ? 8   GLN A CD  1 
ATOM   48   O  OE1 . GLN A 1 8   ? -27.832 8.890   18.761  1.00 25.05 ? 8   GLN A OE1 1 
ATOM   49   N  NE2 . GLN A 1 8   ? -29.353 9.749   20.178  1.00 27.55 ? 8   GLN A NE2 1 
ATOM   50   N  N   . PRO A 1 9   ? -26.310 9.088   25.166  1.00 33.33 ? 9   PRO A N   1 
ATOM   51   C  CA  . PRO A 1 9   ? -26.377 8.145   26.309  1.00 31.88 ? 9   PRO A CA  1 
ATOM   52   C  C   . PRO A 1 9   ? -27.038 6.832   25.868  1.00 34.72 ? 9   PRO A C   1 
ATOM   53   O  O   . PRO A 1 9   ? -27.878 6.797   24.964  1.00 32.24 ? 9   PRO A O   1 
ATOM   54   C  CB  . PRO A 1 9   ? -27.288 8.862   27.306  1.00 34.98 ? 9   PRO A CB  1 
ATOM   55   C  CG  . PRO A 1 9   ? -27.072 10.336  26.969  1.00 40.14 ? 9   PRO A CG  1 
ATOM   56   C  CD  . PRO A 1 9   ? -27.049 10.333  25.426  1.00 36.71 ? 9   PRO A CD  1 
ATOM   57   N  N   . GLY A 1 10  ? -26.662 5.704   26.491  1.00 32.72 ? 10  GLY A N   1 
ATOM   58   C  CA  . GLY A 1 10  ? -27.196 4.421   26.049  1.00 29.65 ? 10  GLY A CA  1 
ATOM   59   C  C   . GLY A 1 10  ? -28.706 4.206   26.312  1.00 33.99 ? 10  GLY A C   1 
ATOM   60   O  O   . GLY A 1 10  ? -29.408 3.620   25.448  1.00 32.11 ? 10  GLY A O   1 
ATOM   61   N  N   . THR A 1 11  ? -29.197 4.541   27.539  1.00 34.27 ? 11  THR A N   1 
ATOM   62   C  CA  . THR A 1 11  ? -30.555 4.169   27.960  1.00 33.85 ? 11  THR A CA  1 
ATOM   63   C  C   . THR A 1 11  ? -31.173 5.262   28.828  1.00 36.04 ? 11  THR A C   1 
ATOM   64   O  O   . THR A 1 11  ? -30.497 5.873   29.662  1.00 36.00 ? 11  THR A O   1 
ATOM   65   C  CB  . THR A 1 11  ? -30.585 2.905   28.848  1.00 34.66 ? 11  THR A CB  1 
ATOM   66   O  OG1 . THR A 1 11  ? -29.541 3.055   29.825  1.00 36.19 ? 11  THR A OG1 1 
ATOM   67   C  CG2 . THR A 1 11  ? -30.241 1.627   28.106  1.00 36.34 ? 11  THR A CG2 1 
ATOM   68   N  N   . GLU A 1 12  ? -32.505 5.356   28.756  1.00 31.54 ? 12  GLU A N   1 
ATOM   69   C  CA  . GLU A 1 12  ? -33.233 6.155   29.717  1.00 33.12 ? 12  GLU A CA  1 
ATOM   70   C  C   . GLU A 1 12  ? -34.424 5.306   30.138  1.00 37.58 ? 12  GLU A C   1 
ATOM   71   O  O   . GLU A 1 12  ? -35.195 4.936   29.262  1.00 30.33 ? 12  GLU A O   1 
ATOM   72   C  CB  . GLU A 1 12  ? -33.761 7.456   29.099  1.00 29.99 ? 12  GLU A CB  1 
ATOM   73   C  CG  . GLU A 1 12  ? -32.629 8.404   28.732  1.00 40.01 ? 12  GLU A CG  1 
ATOM   74   C  CD  . GLU A 1 12  ? -31.853 9.075   29.867  1.00 54.93 ? 12  GLU A CD  1 
ATOM   75   O  OE1 . GLU A 1 12  ? -32.299 9.052   31.045  1.00 51.36 ? 12  GLU A OE1 1 
ATOM   76   O  OE2 . GLU A 1 12  ? -30.759 9.630   29.564  1.00 59.31 ? 12  GLU A OE2 1 
ATOM   77   N  N   . LEU A 1 13  ? -34.533 5.020   31.457  1.00 33.79 ? 13  LEU A N   1 
ATOM   78   C  CA  . LEU A 1 13  ? -35.673 4.266   31.980  1.00 32.41 ? 13  LEU A CA  1 
ATOM   79   C  C   . LEU A 1 13  ? -36.648 5.219   32.676  1.00 34.28 ? 13  LEU A C   1 
ATOM   80   O  O   . LEU A 1 13  ? -36.268 5.842   33.644  1.00 32.84 ? 13  LEU A O   1 
ATOM   81   C  CB  . LEU A 1 13  ? -35.077 3.245   32.928  1.00 32.39 ? 13  LEU A CB  1 
ATOM   82   C  CG  . LEU A 1 13  ? -36.112 2.280   33.518  1.00 32.07 ? 13  LEU A CG  1 
ATOM   83   C  CD1 . LEU A 1 13  ? -36.708 1.348   32.453  1.00 30.83 ? 13  LEU A CD1 1 
ATOM   84   C  CD2 . LEU A 1 13  ? -35.536 1.403   34.638  1.00 33.77 ? 13  LEU A CD2 1 
ATOM   85   N  N   . VAL A 1 14  ? -37.879 5.375   32.162  1.00 29.93 ? 14  VAL A N   1 
ATOM   86   C  CA  . VAL A 1 14  ? -38.717 6.525   32.517  1.00 30.22 ? 14  VAL A CA  1 
ATOM   87   C  C   . VAL A 1 14  ? -40.158 6.062   32.729  1.00 34.37 ? 14  VAL A C   1 
ATOM   88   O  O   . VAL A 1 14  ? -40.559 4.979   32.260  1.00 33.84 ? 14  VAL A O   1 
ATOM   89   C  CB  . VAL A 1 14  ? -38.622 7.550   31.364  1.00 31.18 ? 14  VAL A CB  1 
ATOM   90   C  CG1 . VAL A 1 14  ? -37.205 8.103   31.254  1.00 35.63 ? 14  VAL A CG1 1 
ATOM   91   C  CG2 . VAL A 1 14  ? -39.047 6.924   30.026  1.00 30.70 ? 14  VAL A CG2 1 
ATOM   92   N  N   . LYS A 1 15  ? -40.927 6.877   33.466  1.00 36.01 ? 15  LYS A N   1 
ATOM   93   C  CA  . LYS A 1 15  ? -42.286 6.556   33.880  1.00 36.95 ? 15  LYS A CA  1 
ATOM   94   C  C   . LYS A 1 15  ? -43.269 7.154   32.874  1.00 34.02 ? 15  LYS A C   1 
ATOM   95   O  O   . LYS A 1 15  ? -43.012 8.198   32.255  1.00 35.47 ? 15  LYS A O   1 
ATOM   96   C  CB  . LYS A 1 15  ? -42.624 7.280   35.194  1.00 41.85 ? 15  LYS A CB  1 
ATOM   97   C  CG  . LYS A 1 15  ? -41.611 7.151   36.317  0.60 40.67 ? 15  LYS A CG  1 
ATOM   98   C  CD  . LYS A 1 15  ? -42.000 7.845   37.618  0.60 44.96 ? 15  LYS A CD  1 
ATOM   99   C  CE  . LYS A 1 15  ? -42.893 6.939   38.409  0.60 47.54 ? 15  LYS A CE  1 
ATOM   100  N  NZ  . LYS A 1 15  ? -43.069 7.286   39.825  0.60 52.98 ? 15  LYS A NZ  1 
ATOM   101  N  N   . PRO A 1 16  ? -44.437 6.523   32.655  1.00 32.54 ? 16  PRO A N   1 
ATOM   102  C  CA  . PRO A 1 16  ? -45.478 7.139   31.802  1.00 34.82 ? 16  PRO A CA  1 
ATOM   103  C  C   . PRO A 1 16  ? -45.847 8.511   32.344  1.00 38.37 ? 16  PRO A C   1 
ATOM   104  O  O   . PRO A 1 16  ? -45.840 8.705   33.559  1.00 38.06 ? 16  PRO A O   1 
ATOM   105  C  CB  . PRO A 1 16  ? -46.664 6.181   31.860  1.00 37.33 ? 16  PRO A CB  1 
ATOM   106  C  CG  . PRO A 1 16  ? -46.035 4.870   32.297  1.00 36.90 ? 16  PRO A CG  1 
ATOM   107  C  CD  . PRO A 1 16  ? -44.751 5.156   33.081  1.00 35.09 ? 16  PRO A CD  1 
ATOM   108  N  N   . GLY A 1 17  ? -46.087 9.456   31.423  1.00 37.37 ? 17  GLY A N   1 
ATOM   109  C  CA  . GLY A 1 17  ? -46.532 10.775  31.834  1.00 38.83 ? 17  GLY A CA  1 
ATOM   110  C  C   . GLY A 1 17  ? -45.370 11.718  32.116  1.00 37.50 ? 17  GLY A C   1 
ATOM   111  O  O   . GLY A 1 17  ? -45.586 12.914  32.119  1.00 41.26 ? 17  GLY A O   1 
ATOM   112  N  N   . ALA A 1 18  ? -44.150 11.207  32.355  1.00 38.26 ? 18  ALA A N   1 
ATOM   113  C  CA  . ALA A 1 18  ? -42.988 12.081  32.519  1.00 34.87 ? 18  ALA A CA  1 
ATOM   114  C  C   . ALA A 1 18  ? -42.536 12.667  31.164  1.00 37.09 ? 18  ALA A C   1 
ATOM   115  O  O   . ALA A 1 18  ? -43.128 12.375  30.118  1.00 36.63 ? 18  ALA A O   1 
ATOM   116  C  CB  . ALA A 1 18  ? -41.880 11.285  33.205  1.00 34.20 ? 18  ALA A CB  1 
ATOM   117  N  N   A SER A 1 19  ? -41.552 13.578  31.212  0.70 36.27 ? 19  SER A N   1 
ATOM   118  N  N   B SER A 1 19  ? -41.484 13.497  31.216  0.30 35.64 ? 19  SER A N   1 
ATOM   119  C  CA  A SER A 1 19  ? -40.770 13.986  30.056  0.70 37.36 ? 19  SER A CA  1 
ATOM   120  C  CA  B SER A 1 19  ? -40.783 14.023  30.056  0.30 35.38 ? 19  SER A CA  1 
ATOM   121  C  C   A SER A 1 19  ? -39.352 13.456  30.206  0.70 36.95 ? 19  SER A C   1 
ATOM   122  C  C   B SER A 1 19  ? -39.299 13.701  30.199  0.30 35.79 ? 19  SER A C   1 
ATOM   123  O  O   A SER A 1 19  ? -38.917 13.124  31.308  0.70 34.40 ? 19  SER A O   1 
ATOM   124  O  O   B SER A 1 19  ? -38.761 13.772  31.300  0.30 36.31 ? 19  SER A O   1 
ATOM   125  C  CB  A SER A 1 19  ? -40.729 15.485  29.877  0.70 41.62 ? 19  SER A CB  1 
ATOM   126  C  CB  B SER A 1 19  ? -40.949 15.512  29.974  0.30 35.99 ? 19  SER A CB  1 
ATOM   127  O  OG  A SER A 1 19  ? -42.041 15.977  29.664  0.70 42.79 ? 19  SER A OG  1 
ATOM   128  O  OG  B SER A 1 19  ? -40.298 16.096  31.093  0.30 33.21 ? 19  SER A OG  1 
ATOM   129  N  N   . VAL A 1 20  ? -38.633 13.382  29.082  1.00 34.14 ? 20  VAL A N   1 
ATOM   130  C  CA  . VAL A 1 20  ? -37.229 13.000  29.151  1.00 32.76 ? 20  VAL A CA  1 
ATOM   131  C  C   . VAL A 1 20  ? -36.459 13.877  28.161  1.00 31.91 ? 20  VAL A C   1 
ATOM   132  O  O   . VAL A 1 20  ? -36.972 14.208  27.090  1.00 31.41 ? 20  VAL A O   1 
ATOM   133  C  CB  . VAL A 1 20  ? -37.014 11.490  28.933  1.00 33.40 ? 20  VAL A CB  1 
ATOM   134  C  CG1 . VAL A 1 20  ? -37.455 11.036  27.543  1.00 34.28 ? 20  VAL A CG1 1 
ATOM   135  C  CG2 . VAL A 1 20  ? -35.565 11.106  29.203  1.00 33.22 ? 20  VAL A CG2 1 
ATOM   136  N  N   . ARG A 1 21  ? -35.233 14.258  28.526  1.00 32.60 ? 21  ARG A N   1 
ATOM   137  C  CA  . ARG A 1 21  ? -34.444 15.034  27.582  1.00 33.36 ? 21  ARG A CA  1 
ATOM   138  C  C   . ARG A 1 21  ? -33.285 14.197  27.066  1.00 32.84 ? 21  ARG A C   1 
ATOM   139  O  O   . ARG A 1 21  ? -32.470 13.723  27.866  1.00 33.55 ? 21  ARG A O   1 
ATOM   140  C  CB  . ARG A 1 21  ? -33.879 16.289  28.262  1.00 37.93 ? 21  ARG A CB  1 
ATOM   141  C  CG  . ARG A 1 21  ? -33.435 17.257  27.166  1.00 41.82 ? 21  ARG A CG  1 
ATOM   142  C  CD  . ARG A 1 21  ? -33.140 18.706  27.628  1.00 48.76 ? 21  ARG A CD  1 
ATOM   143  N  NE  . ARG A 1 21  ? -32.040 18.548  28.586  1.00 51.61 ? 21  ARG A NE  1 
ATOM   144  C  CZ  . ARG A 1 21  ? -31.023 19.380  28.743  1.00 54.37 ? 21  ARG A CZ  1 
ATOM   145  N  NH1 . ARG A 1 21  ? -31.050 20.582  28.175  1.00 58.50 ? 21  ARG A NH1 1 
ATOM   146  N  NH2 . ARG A 1 21  ? -29.989 18.969  29.462  1.00 55.36 ? 21  ARG A NH2 1 
ATOM   147  N  N   . LEU A 1 22  ? -33.251 13.974  25.728  1.00 31.60 ? 22  LEU A N   1 
ATOM   148  C  CA  . LEU A 1 22  ? -32.175 13.197  25.126  1.00 31.40 ? 22  LEU A CA  1 
ATOM   149  C  C   . LEU A 1 22  ? -31.080 14.147  24.622  1.00 30.56 ? 22  LEU A C   1 
ATOM   150  O  O   . LEU A 1 22  ? -31.371 15.213  24.104  1.00 31.44 ? 22  LEU A O   1 
ATOM   151  C  CB  . LEU A 1 22  ? -32.736 12.356  23.975  1.00 28.62 ? 22  LEU A CB  1 
ATOM   152  C  CG  . LEU A 1 22  ? -33.924 11.450  24.347  1.00 29.63 ? 22  LEU A CG  1 
ATOM   153  C  CD1 . LEU A 1 22  ? -34.215 10.479  23.185  1.00 30.99 ? 22  LEU A CD1 1 
ATOM   154  C  CD2 . LEU A 1 22  ? -33.559 10.664  25.564  1.00 30.70 ? 22  LEU A CD2 1 
ATOM   155  N  N   . SER A 1 23  ? -29.816 13.733  24.773  1.00 29.65 ? 23  SER A N   1 
ATOM   156  C  CA  . SER A 1 23  ? -28.722 14.595  24.332  1.00 29.32 ? 23  SER A CA  1 
ATOM   157  C  C   . SER A 1 23  ? -27.943 13.952  23.196  1.00 29.14 ? 23  SER A C   1 
ATOM   158  O  O   . SER A 1 23  ? -27.849 12.729  23.072  1.00 28.79 ? 23  SER A O   1 
ATOM   159  C  CB  . SER A 1 23  ? -27.826 14.987  25.467  1.00 31.09 ? 23  SER A CB  1 
ATOM   160  O  OG  . SER A 1 23  ? -27.384 13.827  26.157  1.00 34.83 ? 23  SER A OG  1 
ATOM   161  N  N   . CYS A 1 24  ? -27.316 14.815  22.404  1.00 28.83 ? 24  CYS A N   1 
ATOM   162  C  CA  . CYS A 1 24  ? -26.494 14.413  21.282  1.00 29.24 ? 24  CYS A CA  1 
ATOM   163  C  C   . CYS A 1 24  ? -25.294 15.360  21.305  1.00 31.53 ? 24  CYS A C   1 
ATOM   164  O  O   . CYS A 1 24  ? -25.396 16.469  20.801  1.00 29.58 ? 24  CYS A O   1 
ATOM   165  C  CB  . CYS A 1 24  ? -27.322 14.499  20.005  1.00 28.73 ? 24  CYS A CB  1 
ATOM   166  S  SG  . CYS A 1 24  ? -26.344 14.308  18.490  1.00 32.38 ? 24  CYS A SG  1 
ATOM   167  N  N   . LYS A 1 25  ? -24.197 14.917  21.934  1.00 28.87 ? 25  LYS A N   1 
ATOM   168  C  CA  . LYS A 1 25  ? -22.976 15.710  22.033  1.00 31.38 ? 25  LYS A CA  1 
ATOM   169  C  C   . LYS A 1 25  ? -22.080 15.537  20.814  1.00 32.29 ? 25  LYS A C   1 
ATOM   170  O  O   . LYS A 1 25  ? -21.674 14.403  20.492  1.00 32.17 ? 25  LYS A O   1 
ATOM   171  C  CB  . LYS A 1 25  ? -22.291 15.356  23.366  1.00 31.12 ? 25  LYS A CB  1 
ATOM   172  C  CG  . LYS A 1 25  ? -21.038 16.200  23.633  1.00 36.70 ? 25  LYS A CG  1 
ATOM   173  C  CD  . LYS A 1 25  ? -20.265 15.644  24.833  0.50 38.73 ? 25  LYS A CD  1 
ATOM   174  N  N   . THR A 1 26  ? -21.800 16.669  20.102  1.00 28.03 ? 26  THR A N   1 
ATOM   175  C  CA  . THR A 1 26  ? -21.146 16.573  18.814  1.00 29.11 ? 26  THR A CA  1 
ATOM   176  C  C   . THR A 1 26  ? -19.683 16.944  19.027  1.00 30.28 ? 26  THR A C   1 
ATOM   177  O  O   . THR A 1 26  ? -19.357 17.761  19.902  1.00 30.04 ? 26  THR A O   1 
ATOM   178  C  CB  . THR A 1 26  ? -21.824 17.416  17.716  1.00 28.88 ? 26  THR A CB  1 
ATOM   179  O  OG1 . THR A 1 26  ? -21.394 18.769  17.931  1.00 29.22 ? 26  THR A OG1 1 
ATOM   180  C  CG2 . THR A 1 26  ? -23.351 17.336  17.774  1.00 29.23 ? 26  THR A CG2 1 
ATOM   181  N  N   . SER A 1 27  ? -18.833 16.402  18.167  1.00 30.16 ? 27  SER A N   1 
ATOM   182  C  CA  . SER A 1 27  ? -17.439 16.810  18.140  1.00 32.34 ? 27  SER A CA  1 
ATOM   183  C  C   . SER A 1 27  ? -16.831 16.562  16.766  1.00 32.95 ? 27  SER A C   1 
ATOM   184  O  O   . SER A 1 27  ? -17.344 15.783  15.934  1.00 31.59 ? 27  SER A O   1 
ATOM   185  C  CB  . SER A 1 27  ? -16.615 16.163  19.256  1.00 35.64 ? 27  SER A CB  1 
ATOM   186  O  OG  . SER A 1 27  ? -16.742 14.744  19.130  1.00 37.21 ? 27  SER A OG  1 
ATOM   187  N  N   . GLY A 1 28  ? -15.721 17.277  16.515  1.00 31.80 ? 28  GLY A N   1 
ATOM   188  C  CA  . GLY A 1 28  ? -14.944 16.909  15.333  1.00 33.71 ? 28  GLY A CA  1 
ATOM   189  C  C   . GLY A 1 28  ? -15.337 17.698  14.072  1.00 32.71 ? 28  GLY A C   1 
ATOM   190  O  O   . GLY A 1 28  ? -14.775 17.443  13.027  1.00 34.29 ? 28  GLY A O   1 
ATOM   191  N  N   . TYR A 1 29  ? -16.316 18.609  14.178  1.00 33.21 ? 29  TYR A N   1 
ATOM   192  C  CA  . TYR A 1 29  ? -16.774 19.452  13.069  1.00 30.05 ? 29  TYR A CA  1 
ATOM   193  C  C   . TYR A 1 29  ? -17.494 20.660  13.681  1.00 31.19 ? 29  TYR A C   1 
ATOM   194  O  O   . TYR A 1 29  ? -17.790 20.656  14.878  1.00 30.56 ? 29  TYR A O   1 
ATOM   195  C  CB  . TYR A 1 29  ? -17.680 18.650  12.122  1.00 28.16 ? 29  TYR A CB  1 
ATOM   196  C  CG  . TYR A 1 29  ? -19.075 18.390  12.688  1.00 30.13 ? 29  TYR A CG  1 
ATOM   197  C  CD1 . TYR A 1 29  ? -19.324 17.319  13.554  1.00 27.63 ? 29  TYR A CD1 1 
ATOM   198  C  CD2 . TYR A 1 29  ? -20.121 19.278  12.432  1.00 28.94 ? 29  TYR A CD2 1 
ATOM   199  C  CE1 . TYR A 1 29  ? -20.599 17.113  14.077  1.00 27.42 ? 29  TYR A CE1 1 
ATOM   200  C  CE2 . TYR A 1 29  ? -21.400 19.068  12.922  1.00 28.69 ? 29  TYR A CE2 1 
ATOM   201  C  CZ  . TYR A 1 29  ? -21.643 17.959  13.720  1.00 28.36 ? 29  TYR A CZ  1 
ATOM   202  O  OH  . TYR A 1 29  ? -22.906 17.837  14.213  1.00 28.10 ? 29  TYR A OH  1 
ATOM   203  N  N   . THR A 1 30  ? -17.805 21.702  12.865  1.00 31.87 ? 30  THR A N   1 
ATOM   204  C  CA  . THR A 1 30  ? -18.470 22.893  13.380  1.00 29.75 ? 30  THR A CA  1 
ATOM   205  C  C   . THR A 1 30  ? -19.952 22.634  13.595  1.00 29.54 ? 30  THR A C   1 
ATOM   206  O  O   . THR A 1 30  ? -20.683 22.593  12.587  1.00 29.82 ? 30  THR A O   1 
ATOM   207  C  CB  . THR A 1 30  ? -18.372 24.082  12.408  1.00 32.91 ? 30  THR A CB  1 
ATOM   208  O  OG1 . THR A 1 30  ? -16.963 24.194  12.228  1.00 34.78 ? 30  THR A OG1 1 
ATOM   209  C  CG2 . THR A 1 30  ? -18.948 25.320  13.079  1.00 32.93 ? 30  THR A CG2 1 
ATOM   210  N  N   . PHE A 1 31  ? -20.351 22.538  14.881  1.00 30.79 ? 31  PHE A N   1 
ATOM   211  C  CA  . PHE A 1 31  ? -21.707 22.166  15.277  1.00 28.30 ? 31  PHE A CA  1 
ATOM   212  C  C   . PHE A 1 31  ? -22.712 23.107  14.625  1.00 32.83 ? 31  PHE A C   1 
ATOM   213  O  O   . PHE A 1 31  ? -23.739 22.675  14.110  1.00 28.96 ? 31  PHE A O   1 
ATOM   214  C  CB  . PHE A 1 31  ? -21.762 22.327  16.810  1.00 30.14 ? 31  PHE A CB  1 
ATOM   215  C  CG  . PHE A 1 31  ? -23.146 22.154  17.431  1.00 29.82 ? 31  PHE A CG  1 
ATOM   216  C  CD1 . PHE A 1 31  ? -23.817 20.934  17.325  1.00 32.21 ? 31  PHE A CD1 1 
ATOM   217  C  CD2 . PHE A 1 31  ? -23.766 23.187  18.129  1.00 31.59 ? 31  PHE A CD2 1 
ATOM   218  C  CE1 . PHE A 1 31  ? -25.061 20.744  17.938  1.00 34.49 ? 31  PHE A CE1 1 
ATOM   219  C  CE2 . PHE A 1 31  ? -25.018 23.017  18.725  1.00 30.72 ? 31  PHE A CE2 1 
ATOM   220  C  CZ  . PHE A 1 31  ? -25.673 21.783  18.609  1.00 32.86 ? 31  PHE A CZ  1 
ATOM   221  N  N   . ALA A 1 32  ? -22.391 24.410  14.650  1.00 31.33 ? 32  ALA A N   1 
ATOM   222  C  CA  . ALA A 1 32  ? -23.328 25.427  14.188  1.00 30.36 ? 32  ALA A CA  1 
ATOM   223  C  C   . ALA A 1 32  ? -23.714 25.263  12.725  1.00 30.45 ? 32  ALA A C   1 
ATOM   224  O  O   . ALA A 1 32  ? -24.769 25.780  12.344  1.00 33.88 ? 32  ALA A O   1 
ATOM   225  C  CB  . ALA A 1 32  ? -22.704 26.827  14.404  1.00 30.92 ? 32  ALA A CB  1 
ATOM   226  N  N   . SER A 1 33  ? -22.887 24.575  11.911  1.00 28.31 ? 33  SER A N   1 
ATOM   227  C  CA  . SER A 1 33  ? -23.013 24.693  10.459  1.00 27.82 ? 33  SER A CA  1 
ATOM   228  C  C   . SER A 1 33  ? -23.744 23.543  9.739   1.00 27.16 ? 33  SER A C   1 
ATOM   229  O  O   . SER A 1 33  ? -23.898 23.638  8.503   1.00 26.31 ? 33  SER A O   1 
ATOM   230  C  CB  . SER A 1 33  ? -21.656 24.911  9.835   1.00 30.05 ? 33  SER A CB  1 
ATOM   231  O  OG  . SER A 1 33  ? -21.086 26.142  10.294  1.00 31.49 ? 33  SER A OG  1 
ATOM   232  N  N   . TYR A 1 34  ? -24.231 22.508  10.468  1.00 28.92 ? 34  TYR A N   1 
ATOM   233  C  CA  . TYR A 1 34  ? -24.841 21.369  9.760   1.00 27.52 ? 34  TYR A CA  1 
ATOM   234  C  C   . TYR A 1 34  ? -26.132 20.998  10.489  1.00 30.26 ? 34  TYR A C   1 
ATOM   235  O  O   . TYR A 1 34  ? -26.150 20.909  11.716  1.00 30.75 ? 34  TYR A O   1 
ATOM   236  C  CB  . TYR A 1 34  ? -23.929 20.141  9.891   1.00 27.61 ? 34  TYR A CB  1 
ATOM   237  C  CG  . TYR A 1 34  ? -22.666 20.302  9.057   1.00 25.60 ? 34  TYR A CG  1 
ATOM   238  C  CD1 . TYR A 1 34  ? -21.553 20.998  9.568   1.00 25.67 ? 34  TYR A CD1 1 
ATOM   239  C  CD2 . TYR A 1 34  ? -22.619 19.786  7.762   1.00 27.03 ? 34  TYR A CD2 1 
ATOM   240  C  CE1 . TYR A 1 34  ? -20.425 21.205  8.775   1.00 26.31 ? 34  TYR A CE1 1 
ATOM   241  C  CE2 . TYR A 1 34  ? -21.490 19.973  6.971   1.00 26.13 ? 34  TYR A CE2 1 
ATOM   242  C  CZ  . TYR A 1 34  ? -20.414 20.692  7.478   1.00 27.82 ? 34  TYR A CZ  1 
ATOM   243  O  OH  . TYR A 1 34  ? -19.366 20.857  6.594   1.00 28.45 ? 34  TYR A OH  1 
ATOM   244  N  N   . THR A 1 35  ? -27.196 20.792  9.722   1.00 28.78 ? 35  THR A N   1 
ATOM   245  C  CA  . THR A 1 35  ? -28.477 20.397  10.290  1.00 27.65 ? 35  THR A CA  1 
ATOM   246  C  C   . THR A 1 35  ? -28.298 19.048  11.003  1.00 27.54 ? 35  THR A C   1 
ATOM   247  O  O   . THR A 1 35  ? -27.639 18.154  10.484  1.00 25.20 ? 35  THR A O   1 
ATOM   248  C  CB  . THR A 1 35  ? -29.407 20.244  9.077   1.00 28.33 ? 35  THR A CB  1 
ATOM   249  O  OG1 . THR A 1 35  ? -29.589 21.564  8.538   1.00 30.57 ? 35  THR A OG1 1 
ATOM   250  C  CG2 . THR A 1 35  ? -30.793 19.771  9.498   1.00 27.38 ? 35  THR A CG2 1 
ATOM   251  N  N   . LEU A 1 36  ? -29.038 18.856  12.099  1.00 26.49 ? 36  LEU A N   1 
ATOM   252  C  CA  . LEU A 1 36  ? -29.081 17.530  12.714  1.00 28.63 ? 36  LEU A CA  1 
ATOM   253  C  C   . LEU A 1 36  ? -30.532 17.079  12.739  1.00 29.15 ? 36  LEU A C   1 
ATOM   254  O  O   . LEU A 1 36  ? -31.456 17.884  12.952  1.00 30.06 ? 36  LEU A O   1 
ATOM   255  C  CB  . LEU A 1 36  ? -28.540 17.639  14.138  1.00 28.09 ? 36  LEU A CB  1 
ATOM   256  C  CG  . LEU A 1 36  ? -27.018 17.748  14.257  1.00 33.43 ? 36  LEU A CG  1 
ATOM   257  C  CD1 . LEU A 1 36  ? -26.674 18.178  15.703  1.00 32.17 ? 36  LEU A CD1 1 
ATOM   258  C  CD2 . LEU A 1 36  ? -26.277 16.448  13.959  1.00 34.93 ? 36  LEU A CD2 1 
ATOM   259  N  N   . HIS A 1 37  ? -30.708 15.775  12.515  1.00 25.38 ? 37  HIS A N   1 
ATOM   260  C  CA  . HIS A 1 37  ? -32.006 15.152  12.434  1.00 25.19 ? 37  HIS A CA  1 
ATOM   261  C  C   . HIS A 1 37  ? -32.142 14.148  13.577  1.00 24.46 ? 37  HIS A C   1 
ATOM   262  O  O   . HIS A 1 37  ? -31.154 13.649  14.125  1.00 24.75 ? 37  HIS A O   1 
ATOM   263  C  CB  . HIS A 1 37  ? -32.077 14.298  11.157  1.00 24.63 ? 37  HIS A CB  1 
ATOM   264  C  CG  . HIS A 1 37  ? -31.900 15.148  9.926   1.00 25.73 ? 37  HIS A CG  1 
ATOM   265  N  ND1 . HIS A 1 37  ? -32.991 15.567  9.180   1.00 26.21 ? 37  HIS A ND1 1 
ATOM   266  C  CD2 . HIS A 1 37  ? -30.791 15.742  9.347   1.00 24.74 ? 37  HIS A CD2 1 
ATOM   267  C  CE1 . HIS A 1 37  ? -32.561 16.349  8.184   1.00 28.23 ? 37  HIS A CE1 1 
ATOM   268  N  NE2 . HIS A 1 37  ? -31.248 16.451  8.231   1.00 25.16 ? 37  HIS A NE2 1 
ATOM   269  N  N   . TRP A 1 38  ? -33.383 13.891  13.971  1.00 26.69 ? 38  TRP A N   1 
ATOM   270  C  CA  . TRP A 1 38  ? -33.680 12.851  14.951  1.00 25.44 ? 38  TRP A CA  1 
ATOM   271  C  C   . TRP A 1 38  ? -34.629 11.818  14.356  1.00 25.04 ? 38  TRP A C   1 
ATOM   272  O  O   . TRP A 1 38  ? -35.529 12.182  13.597  1.00 25.43 ? 38  TRP A O   1 
ATOM   273  C  CB  . TRP A 1 38  ? -34.313 13.473  16.196  1.00 27.75 ? 38  TRP A CB  1 
ATOM   274  C  CG  . TRP A 1 38  ? -33.365 14.344  16.988  1.00 28.89 ? 38  TRP A CG  1 
ATOM   275  C  CD1 . TRP A 1 38  ? -33.076 15.669  16.725  1.00 31.32 ? 38  TRP A CD1 1 
ATOM   276  C  CD2 . TRP A 1 38  ? -32.621 13.985  18.158  1.00 29.10 ? 38  TRP A CD2 1 
ATOM   277  N  NE1 . TRP A 1 38  ? -32.198 16.136  17.646  1.00 31.02 ? 38  TRP A NE1 1 
ATOM   278  C  CE2 . TRP A 1 38  ? -31.890 15.142  18.541  1.00 31.30 ? 38  TRP A CE2 1 
ATOM   279  C  CE3 . TRP A 1 38  ? -32.488 12.806  18.913  1.00 27.54 ? 38  TRP A CE3 1 
ATOM   280  C  CZ2 . TRP A 1 38  ? -31.073 15.134  19.682  1.00 33.28 ? 38  TRP A CZ2 1 
ATOM   281  C  CZ3 . TRP A 1 38  ? -31.685 12.800  20.049  1.00 29.74 ? 38  TRP A CZ3 1 
ATOM   282  C  CH2 . TRP A 1 38  ? -30.996 13.959  20.421  1.00 32.18 ? 38  TRP A CH2 1 
ATOM   283  N  N   . VAL A 1 39  ? -34.379 10.541  14.682  1.00 23.87 ? 39  VAL A N   1 
ATOM   284  C  CA  . VAL A 1 39  ? -35.009 9.402   14.040  1.00 24.33 ? 39  VAL A CA  1 
ATOM   285  C  C   . VAL A 1 39  ? -35.439 8.407   15.118  1.00 23.73 ? 39  VAL A C   1 
ATOM   286  O  O   . VAL A 1 39  ? -34.619 8.089   16.004  1.00 23.89 ? 39  VAL A O   1 
ATOM   287  C  CB  . VAL A 1 39  ? -34.034 8.736   13.041  1.00 24.86 ? 39  VAL A CB  1 
ATOM   288  C  CG1 . VAL A 1 39  ? -34.649 7.447   12.467  1.00 26.95 ? 39  VAL A CG1 1 
ATOM   289  C  CG2 . VAL A 1 39  ? -33.668 9.648   11.873  1.00 27.53 ? 39  VAL A CG2 1 
ATOM   290  N  N   . LYS A 1 40  ? -36.687 7.919   15.042  1.00 24.61 ? 40  LYS A N   1 
ATOM   291  C  CA  . LYS A 1 40  ? -37.199 6.904   15.989  1.00 23.52 ? 40  LYS A CA  1 
ATOM   292  C  C   . LYS A 1 40  ? -37.138 5.513   15.345  1.00 24.67 ? 40  LYS A C   1 
ATOM   293  O  O   . LYS A 1 40  ? -37.491 5.361   14.186  1.00 24.48 ? 40  LYS A O   1 
ATOM   294  C  CB  . LYS A 1 40  ? -38.682 7.215   16.230  1.00 24.45 ? 40  LYS A CB  1 
ATOM   295  C  CG  . LYS A 1 40  ? -39.339 6.269   17.281  1.00 25.30 ? 40  LYS A CG  1 
ATOM   296  C  CD  . LYS A 1 40  ? -40.766 6.742   17.520  1.00 28.72 ? 40  LYS A CD  1 
ATOM   297  C  CE  . LYS A 1 40  ? -41.543 5.798   18.401  1.00 28.73 ? 40  LYS A CE  1 
ATOM   298  N  NZ  . LYS A 1 40  ? -42.883 6.327   18.715  1.00 30.97 ? 40  LYS A NZ  1 
ATOM   299  N  N   . GLN A 1 41  ? -36.672 4.470   16.071  1.00 23.80 ? 41  GLN A N   1 
ATOM   300  C  CA  . GLN A 1 41  ? -36.653 3.139   15.482  1.00 23.30 ? 41  GLN A CA  1 
ATOM   301  C  C   . GLN A 1 41  ? -37.511 2.251   16.393  1.00 25.82 ? 41  GLN A C   1 
ATOM   302  O  O   . GLN A 1 41  ? -37.336 2.285   17.632  1.00 26.80 ? 41  GLN A O   1 
ATOM   303  C  CB  . GLN A 1 41  ? -35.200 2.677   15.658  1.00 23.75 ? 41  GLN A CB  1 
ATOM   304  C  CG  . GLN A 1 41  ? -34.989 1.214   15.266  1.00 23.40 ? 41  GLN A CG  1 
ATOM   305  C  CD  . GLN A 1 41  ? -33.520 0.833   15.383  1.00 23.26 ? 41  GLN A CD  1 
ATOM   306  O  OE1 . GLN A 1 41  ? -32.884 0.998   16.428  1.00 26.03 ? 41  GLN A OE1 1 
ATOM   307  N  NE2 . GLN A 1 41  ? -32.917 0.357   14.292  1.00 25.00 ? 41  GLN A NE2 1 
ATOM   308  N  N   . THR A 1 42  ? -38.381 1.446   15.754  1.00 27.32 ? 42  THR A N   1 
ATOM   309  C  CA  . THR A 1 42  ? -39.124 0.388   16.433  1.00 26.09 ? 42  THR A CA  1 
ATOM   310  C  C   . THR A 1 42  ? -39.054 -0.870  15.586  1.00 29.33 ? 42  THR A C   1 
ATOM   311  O  O   . THR A 1 42  ? -38.759 -0.789  14.400  1.00 29.43 ? 42  THR A O   1 
ATOM   312  C  CB  . THR A 1 42  ? -40.587 0.764   16.625  1.00 29.52 ? 42  THR A CB  1 
ATOM   313  O  OG1 . THR A 1 42  ? -41.141 1.070   15.358  1.00 31.96 ? 42  THR A OG1 1 
ATOM   314  C  CG2 . THR A 1 42  ? -40.772 2.036   17.428  1.00 33.41 ? 42  THR A CG2 1 
ATOM   315  N  N   . PRO A 1 43  ? -39.279 -2.081  16.176  1.00 33.09 ? 43  PRO A N   1 
ATOM   316  C  CA  . PRO A 1 43  ? -39.219 -3.328  15.383  1.00 35.43 ? 43  PRO A CA  1 
ATOM   317  C  C   . PRO A 1 43  ? -40.238 -3.376  14.218  1.00 46.62 ? 43  PRO A C   1 
ATOM   318  O  O   . PRO A 1 43  ? -39.928 -3.791  13.085  1.00 48.71 ? 43  PRO A O   1 
ATOM   319  C  CB  . PRO A 1 43  ? -39.497 -4.426  16.436  1.00 39.10 ? 43  PRO A CB  1 
ATOM   320  C  CG  . PRO A 1 43  ? -39.199 -3.767  17.780  1.00 31.58 ? 43  PRO A CG  1 
ATOM   321  C  CD  . PRO A 1 43  ? -39.483 -2.266  17.622  1.00 31.60 ? 43  PRO A CD  1 
ATOM   322  N  N   . GLY A 1 44  ? -41.457 -2.874  14.479  1.00 40.81 ? 44  GLY A N   1 
ATOM   323  C  CA  . GLY A 1 44  ? -42.572 -3.009  13.545  1.00 42.36 ? 44  GLY A CA  1 
ATOM   324  C  C   . GLY A 1 44  ? -42.702 -1.867  12.539  1.00 47.50 ? 44  GLY A C   1 
ATOM   325  O  O   . GLY A 1 44  ? -43.189 -2.088  11.436  1.00 53.51 ? 44  GLY A O   1 
ATOM   326  N  N   . GLN A 1 45  ? -42.287 -0.652  12.912  1.00 39.01 ? 45  GLN A N   1 
ATOM   327  C  CA  . GLN A 1 45  ? -42.424 0.477   11.992  1.00 36.34 ? 45  GLN A CA  1 
ATOM   328  C  C   . GLN A 1 45  ? -41.077 0.881   11.427  1.00 38.41 ? 45  GLN A C   1 
ATOM   329  O  O   . GLN A 1 45  ? -41.019 1.859   10.686  1.00 45.12 ? 45  GLN A O   1 
ATOM   330  C  CB  . GLN A 1 45  ? -43.248 1.650   12.534  1.00 41.65 ? 45  GLN A CB  1 
ATOM   331  C  CG  . GLN A 1 45  ? -44.746 1.327   12.591  0.70 44.13 ? 45  GLN A CG  1 
ATOM   332  C  CD  . GLN A 1 45  ? -45.621 2.346   13.305  0.70 47.25 ? 45  GLN A CD  1 
ATOM   333  O  OE1 . GLN A 1 45  ? -45.276 3.521   13.490  0.70 42.78 ? 45  GLN A OE1 1 
ATOM   334  N  NE2 . GLN A 1 45  ? -46.796 1.888   13.716  0.70 51.47 ? 45  GLN A NE2 1 
ATOM   335  N  N   . GLY A 1 46  ? -39.994 0.153   11.735  1.00 32.02 ? 46  GLY A N   1 
ATOM   336  C  CA  . GLY A 1 46  ? -38.749 0.612   11.126  1.00 31.45 ? 46  GLY A CA  1 
ATOM   337  C  C   . GLY A 1 46  ? -38.328 1.991   11.653  1.00 33.13 ? 46  GLY A C   1 
ATOM   338  O  O   . GLY A 1 46  ? -38.345 2.241   12.854  1.00 28.44 ? 46  GLY A O   1 
ATOM   339  N  N   . LEU A 1 47  ? -37.923 2.896   10.756  1.00 27.68 ? 47  LEU A N   1 
ATOM   340  C  CA  . LEU A 1 47  ? -37.392 4.192   11.168  1.00 24.50 ? 47  LEU A CA  1 
ATOM   341  C  C   . LEU A 1 47  ? -38.435 5.246   10.808  1.00 27.30 ? 47  LEU A C   1 
ATOM   342  O  O   . LEU A 1 47  ? -39.119 5.138   9.795   1.00 30.39 ? 47  LEU A O   1 
ATOM   343  C  CB  . LEU A 1 47  ? -36.045 4.450   10.491  1.00 26.07 ? 47  LEU A CB  1 
ATOM   344  C  CG  . LEU A 1 47  ? -34.924 3.427   10.744  1.00 26.31 ? 47  LEU A CG  1 
ATOM   345  C  CD1 . LEU A 1 47  ? -33.714 3.862   9.937   1.00 30.95 ? 47  LEU A CD1 1 
ATOM   346  C  CD2 . LEU A 1 47  ? -34.599 3.386   12.215  1.00 28.61 ? 47  LEU A CD2 1 
ATOM   347  N  N   . ASP A 1 48  ? -38.516 6.268   11.663  1.00 27.07 ? 48  ASP A N   1 
ATOM   348  C  CA  . ASP A 1 48  ? -39.438 7.372   11.476  1.00 27.18 ? 48  ASP A CA  1 
ATOM   349  C  C   . ASP A 1 48  ? -38.657 8.684   11.679  1.00 26.70 ? 48  ASP A C   1 
ATOM   350  O  O   . ASP A 1 48  ? -38.036 8.865   12.710  1.00 28.52 ? 48  ASP A O   1 
ATOM   351  C  CB  . ASP A 1 48  ? -40.555 7.237   12.492  1.00 33.41 ? 48  ASP A CB  1 
ATOM   352  C  CG  . ASP A 1 48  ? -41.949 7.402   11.923  1.00 48.04 ? 48  ASP A CG  1 
ATOM   353  O  OD1 . ASP A 1 48  ? -42.106 8.239   11.024  1.00 58.94 ? 48  ASP A OD1 1 
ATOM   354  O  OD2 . ASP A 1 48  ? -42.863 6.750   12.420  1.00 46.68 ? 48  ASP A OD2 1 
ATOM   355  N  N   . TRP A 1 49  ? -38.775 9.611   10.706  1.00 26.78 ? 49  TRP A N   1 
ATOM   356  C  CA  . TRP A 1 49  ? -38.115 10.905  10.816  1.00 25.72 ? 49  TRP A CA  1 
ATOM   357  C  C   . TRP A 1 49  ? -38.928 11.785  11.762  1.00 26.57 ? 49  TRP A C   1 
ATOM   358  O  O   . TRP A 1 49  ? -40.092 12.051  11.485  1.00 28.66 ? 49  TRP A O   1 
ATOM   359  C  CB  . TRP A 1 49  ? -37.998 11.554  9.427   1.00 24.88 ? 49  TRP A CB  1 
ATOM   360  C  CG  . TRP A 1 49  ? -37.284 12.872  9.466   1.00 26.19 ? 49  TRP A CG  1 
ATOM   361  C  CD1 . TRP A 1 49  ? -35.950 13.124  9.622   1.00 29.09 ? 49  TRP A CD1 1 
ATOM   362  C  CD2 . TRP A 1 49  ? -37.928 14.173  9.343   1.00 25.87 ? 49  TRP A CD2 1 
ATOM   363  N  NE1 . TRP A 1 49  ? -35.711 14.488  9.517   1.00 27.60 ? 49  TRP A NE1 1 
ATOM   364  C  CE2 . TRP A 1 49  ? -36.912 15.146  9.389   1.00 28.14 ? 49  TRP A CE2 1 
ATOM   365  C  CE3 . TRP A 1 49  ? -39.254 14.583  9.197   1.00 30.92 ? 49  TRP A CE3 1 
ATOM   366  C  CZ2 . TRP A 1 49  ? -37.191 16.514  9.275   1.00 30.69 ? 49  TRP A CZ2 1 
ATOM   367  C  CZ3 . TRP A 1 49  ? -39.529 15.935  9.103   1.00 32.27 ? 49  TRP A CZ3 1 
ATOM   368  C  CH2 . TRP A 1 49  ? -38.507 16.883  9.125   1.00 30.21 ? 49  TRP A CH2 1 
ATOM   369  N  N   . ILE A 1 50  ? -38.302 12.257  12.844  1.00 28.03 ? 50  ILE A N   1 
ATOM   370  C  CA  . ILE A 1 50  ? -38.980 13.090  13.835  1.00 26.57 ? 50  ILE A CA  1 
ATOM   371  C  C   . ILE A 1 50  ? -38.941 14.556  13.434  1.00 28.28 ? 50  ILE A C   1 
ATOM   372  O  O   . ILE A 1 50  ? -39.977 15.241  13.458  1.00 27.83 ? 50  ILE A O   1 
ATOM   373  C  CB  . ILE A 1 50  ? -38.360 12.893  15.224  1.00 25.37 ? 50  ILE A CB  1 
ATOM   374  C  CG1 . ILE A 1 50  ? -38.697 11.504  15.728  1.00 24.72 ? 50  ILE A CG1 1 
ATOM   375  C  CG2 . ILE A 1 50  ? -38.827 14.000  16.184  1.00 26.93 ? 50  ILE A CG2 1 
ATOM   376  C  CD1 . ILE A 1 50  ? -37.845 11.098  16.950  1.00 24.94 ? 50  ILE A CD1 1 
ATOM   377  N  N   . GLY A 1 51  ? -37.745 15.038  13.117  1.00 25.69 ? 51  GLY A N   1 
ATOM   378  C  CA  . GLY A 1 51  ? -37.606 16.453  12.812  1.00 26.99 ? 51  GLY A CA  1 
ATOM   379  C  C   . GLY A 1 51  ? -36.131 16.778  12.681  1.00 26.60 ? 51  GLY A C   1 
ATOM   380  O  O   . GLY A 1 51  ? -35.298 15.892  12.876  1.00 27.94 ? 51  GLY A O   1 
ATOM   381  N  N   . ALA A 1 52  ? -35.820 18.061  12.466  1.00 24.82 ? 52  ALA A N   1 
ATOM   382  C  CA  . ALA A 1 52  ? -34.441 18.476  12.234  1.00 25.04 ? 52  ALA A CA  1 
ATOM   383  C  C   . ALA A 1 52  ? -34.268 19.874  12.850  1.00 28.34 ? 52  ALA A C   1 
ATOM   384  O  O   . ALA A 1 52  ? -35.232 20.652  12.904  1.00 28.65 ? 52  ALA A O   1 
ATOM   385  C  CB  . ALA A 1 52  ? -34.085 18.484  10.738  1.00 28.32 ? 52  ALA A CB  1 
ATOM   386  N  N   . ILE A 1 53  ? -33.038 20.195  13.215  1.00 25.21 ? 53  ILE A N   1 
ATOM   387  C  CA  . ILE A 1 53  ? -32.703 21.527  13.720  1.00 27.14 ? 53  ILE A CA  1 
ATOM   388  C  C   . ILE A 1 53  ? -31.439 22.001  13.022  1.00 27.62 ? 53  ILE A C   1 
ATOM   389  O  O   . ILE A 1 53  ? -30.531 21.187  12.792  1.00 28.68 ? 53  ILE A O   1 
ATOM   390  C  CB  . ILE A 1 53  ? -32.508 21.526  15.258  1.00 28.81 ? 53  ILE A CB  1 
ATOM   391  C  CG1 . ILE A 1 53  ? -32.286 22.968  15.852  1.00 29.22 ? 53  ILE A CG1 1 
ATOM   392  C  CG2 . ILE A 1 53  ? -31.372 20.580  15.724  1.00 29.68 ? 53  ILE A CG2 1 
ATOM   393  C  CD1 . ILE A 1 53  ? -32.533 23.016  17.371  1.00 30.34 ? 53  ILE A CD1 1 
ATOM   394  N  N   . TYR A 1 54  ? -31.369 23.320  12.694  1.00 28.28 ? 54  TYR A N   1 
ATOM   395  C  CA  . TYR A 1 54  ? -30.117 23.908  12.261  1.00 29.24 ? 54  TYR A CA  1 
ATOM   396  C  C   . TYR A 1 54  ? -29.458 24.575  13.457  1.00 30.19 ? 54  TYR A C   1 
ATOM   397  O  O   . TYR A 1 54  ? -29.988 25.582  13.921  1.00 33.01 ? 54  TYR A O   1 
ATOM   398  C  CB  . TYR A 1 54  ? -30.350 24.959  11.153  1.00 27.88 ? 54  TYR A CB  1 
ATOM   399  C  CG  . TYR A 1 54  ? -29.032 25.494  10.595  1.00 28.39 ? 54  TYR A CG  1 
ATOM   400  C  CD1 . TYR A 1 54  ? -28.153 24.661  9.903   1.00 28.70 ? 54  TYR A CD1 1 
ATOM   401  C  CD2 . TYR A 1 54  ? -28.601 26.795  10.889  1.00 30.59 ? 54  TYR A CD2 1 
ATOM   402  C  CE1 . TYR A 1 54  ? -26.944 25.115  9.383   1.00 30.69 ? 54  TYR A CE1 1 
ATOM   403  C  CE2 . TYR A 1 54  ? -27.379 27.240  10.420  1.00 32.36 ? 54  TYR A CE2 1 
ATOM   404  C  CZ  . TYR A 1 54  ? -26.571 26.427  9.647   1.00 31.20 ? 54  TYR A CZ  1 
ATOM   405  O  OH  . TYR A 1 54  ? -25.354 26.916  9.243   1.00 34.99 ? 54  TYR A OH  1 
ATOM   406  N  N   . PRO A 1 55  ? -28.349 24.031  14.036  1.00 29.39 ? 55  PRO A N   1 
ATOM   407  C  CA  . PRO A 1 55  ? -27.865 24.536  15.329  1.00 29.93 ? 55  PRO A CA  1 
ATOM   408  C  C   . PRO A 1 55  ? -27.412 26.007  15.308  1.00 35.14 ? 55  PRO A C   1 
ATOM   409  O  O   . PRO A 1 55  ? -27.465 26.684  16.328  1.00 35.89 ? 55  PRO A O   1 
ATOM   410  C  CB  . PRO A 1 55  ? -26.700 23.556  15.659  1.00 30.08 ? 55  PRO A CB  1 
ATOM   411  C  CG  . PRO A 1 55  ? -27.089 22.243  14.924  1.00 27.74 ? 55  PRO A CG  1 
ATOM   412  C  CD  . PRO A 1 55  ? -27.658 22.797  13.612  1.00 28.19 ? 55  PRO A CD  1 
ATOM   413  N  N   . GLY A 1 56  ? -26.963 26.484  14.141  1.00 33.90 ? 56  GLY A N   1 
ATOM   414  C  CA  . GLY A 1 56  ? -26.470 27.847  13.989  1.00 37.75 ? 56  GLY A CA  1 
ATOM   415  C  C   . GLY A 1 56  ? -27.474 28.896  14.487  1.00 42.24 ? 56  GLY A C   1 
ATOM   416  O  O   . GLY A 1 56  ? -27.088 29.907  15.070  1.00 39.43 ? 56  GLY A O   1 
ATOM   417  N  N   . ASN A 1 57  ? -28.766 28.685  14.229  1.00 41.18 ? 57  ASN A N   1 
ATOM   418  C  CA  . ASN A 1 57  ? -29.767 29.695  14.553  1.00 41.06 ? 57  ASN A CA  1 
ATOM   419  C  C   . ASN A 1 57  ? -30.942 29.065  15.300  1.00 40.68 ? 57  ASN A C   1 
ATOM   420  O  O   . ASN A 1 57  ? -31.870 29.760  15.687  1.00 39.39 ? 57  ASN A O   1 
ATOM   421  C  CB  . ASN A 1 57  ? -30.204 30.474  13.313  1.00 40.41 ? 57  ASN A CB  1 
ATOM   422  C  CG  . ASN A 1 57  ? -30.873 29.627  12.256  1.00 41.03 ? 57  ASN A CG  1 
ATOM   423  O  OD1 . ASN A 1 57  ? -31.289 28.496  12.531  1.00 38.47 ? 57  ASN A OD1 1 
ATOM   424  N  ND2 . ASN A 1 57  ? -31.013 30.148  11.049  1.00 39.62 ? 57  ASN A ND2 1 
ATOM   425  N  N   . GLY A 1 58  ? -30.955 27.732  15.463  1.00 34.27 ? 58  GLY A N   1 
ATOM   426  C  CA  . GLY A 1 58  ? -32.029 27.150  16.260  1.00 35.14 ? 58  GLY A CA  1 
ATOM   427  C  C   . GLY A 1 58  ? -33.343 26.899  15.500  1.00 35.25 ? 58  GLY A C   1 
ATOM   428  O  O   . GLY A 1 58  ? -34.319 26.462  16.107  1.00 34.34 ? 58  GLY A O   1 
ATOM   429  N  N   . ASP A 1 59  ? -33.374 27.128  14.189  1.00 34.81 ? 59  ASP A N   1 
ATOM   430  C  CA  . ASP A 1 59  ? -34.539 26.864  13.349  1.00 34.45 ? 59  ASP A CA  1 
ATOM   431  C  C   . ASP A 1 59  ? -34.858 25.362  13.353  1.00 32.92 ? 59  ASP A C   1 
ATOM   432  O  O   . ASP A 1 59  ? -33.940 24.557  13.272  1.00 34.16 ? 59  ASP A O   1 
ATOM   433  C  CB  . ASP A 1 59  ? -34.263 27.287  11.910  1.00 33.70 ? 59  ASP A CB  1 
ATOM   434  C  CG  . ASP A 1 59  ? -34.320 28.788  11.630  0.90 40.39 ? 59  ASP A CG  1 
ATOM   435  O  OD1 . ASP A 1 59  ? -34.581 29.543  12.588  0.90 40.58 ? 59  ASP A OD1 1 
ATOM   436  O  OD2 . ASP A 1 59  ? -34.138 29.168  10.454  0.90 41.02 ? 59  ASP A OD2 1 
ATOM   437  N  N   . THR A 1 60  ? -36.148 24.997  13.435  1.00 33.63 ? 60  THR A N   1 
ATOM   438  C  CA  . THR A 1 60  ? -36.525 23.582  13.518  1.00 31.95 ? 60  THR A CA  1 
ATOM   439  C  C   . THR A 1 60  ? -37.577 23.273  12.465  1.00 34.55 ? 60  THR A C   1 
ATOM   440  O  O   . THR A 1 60  ? -38.317 24.183  12.063  1.00 35.84 ? 60  THR A O   1 
ATOM   441  C  CB  . THR A 1 60  ? -37.058 23.286  14.926  1.00 34.45 ? 60  THR A CB  1 
ATOM   442  O  OG1 . THR A 1 60  ? -38.026 24.274  15.282  1.00 36.78 ? 60  THR A OG1 1 
ATOM   443  C  CG2 . THR A 1 60  ? -35.979 23.304  15.984  1.00 32.21 ? 60  THR A CG2 1 
ATOM   444  N  N   . SER A 1 61  ? -37.641 22.016  11.989  1.00 30.38 ? 61  SER A N   1 
ATOM   445  C  CA  . SER A 1 61  ? -38.767 21.467  11.231  1.00 30.79 ? 61  SER A CA  1 
ATOM   446  C  C   . SER A 1 61  ? -39.182 20.153  11.861  1.00 30.58 ? 61  SER A C   1 
ATOM   447  O  O   . SER A 1 61  ? -38.310 19.418  12.311  1.00 30.79 ? 61  SER A O   1 
ATOM   448  C  CB  . SER A 1 61  ? -38.443 21.192  9.779   1.00 36.28 ? 61  SER A CB  1 
ATOM   449  O  OG  . SER A 1 61  ? -38.076 22.425  9.185   1.00 48.76 ? 61  SER A OG  1 
ATOM   450  N  N   . TYR A 1 62  ? -40.485 19.916  11.932  1.00 32.35 ? 62  TYR A N   1 
ATOM   451  C  CA  . TYR A 1 62  ? -40.984 18.713  12.584  1.00 32.02 ? 62  TYR A CA  1 
ATOM   452  C  C   . TYR A 1 62  ? -41.887 17.949  11.632  1.00 32.29 ? 62  TYR A C   1 
ATOM   453  O  O   . TYR A 1 62  ? -42.599 18.538  10.818  1.00 32.72 ? 62  TYR A O   1 
ATOM   454  C  CB  . TYR A 1 62  ? -41.871 19.014  13.791  1.00 31.73 ? 62  TYR A CB  1 
ATOM   455  C  CG  . TYR A 1 62  ? -41.102 19.658  14.935  1.00 32.69 ? 62  TYR A CG  1 
ATOM   456  C  CD1 . TYR A 1 62  ? -40.905 21.043  14.994  1.00 35.22 ? 62  TYR A CD1 1 
ATOM   457  C  CD2 . TYR A 1 62  ? -40.550 18.864  15.944  1.00 33.81 ? 62  TYR A CD2 1 
ATOM   458  C  CE1 . TYR A 1 62  ? -40.215 21.612  16.055  1.00 37.90 ? 62  TYR A CE1 1 
ATOM   459  C  CE2 . TYR A 1 62  ? -39.864 19.426  17.013  1.00 34.79 ? 62  TYR A CE2 1 
ATOM   460  C  CZ  . TYR A 1 62  ? -39.674 20.799  17.045  1.00 33.27 ? 62  TYR A CZ  1 
ATOM   461  O  OH  . TYR A 1 62  ? -38.957 21.360  18.054  1.00 34.56 ? 62  TYR A OH  1 
ATOM   462  N  N   . ASN A 1 63  ? -41.804 16.623  11.692  1.00 30.31 ? 63  ASN A N   1 
ATOM   463  C  CA  . ASN A 1 63  ? -42.799 15.746  11.108  1.00 32.37 ? 63  ASN A CA  1 
ATOM   464  C  C   . ASN A 1 63  ? -44.104 16.041  11.848  1.00 32.83 ? 63  ASN A C   1 
ATOM   465  O  O   . ASN A 1 63  ? -44.108 16.160  13.079  1.00 33.19 ? 63  ASN A O   1 
ATOM   466  C  CB  . ASN A 1 63  ? -42.376 14.302  11.356  1.00 31.69 ? 63  ASN A CB  1 
ATOM   467  C  CG  . ASN A 1 63  ? -43.213 13.286  10.631  1.00 35.65 ? 63  ASN A CG  1 
ATOM   468  O  OD1 . ASN A 1 63  ? -44.402 13.531  10.373  1.00 35.44 ? 63  ASN A OD1 1 
ATOM   469  N  ND2 . ASN A 1 63  ? -42.624 12.127  10.345  1.00 30.64 ? 63  ASN A ND2 1 
ATOM   470  N  N   . GLN A 1 64  ? -45.180 16.295  11.081  1.00 32.13 ? 64  GLN A N   1 
ATOM   471  C  CA  . GLN A 1 64  ? -46.476 16.624  11.660  1.00 37.79 ? 64  GLN A CA  1 
ATOM   472  C  C   . GLN A 1 64  ? -46.810 15.620  12.766  1.00 37.19 ? 64  GLN A C   1 
ATOM   473  O  O   . GLN A 1 64  ? -47.315 15.975  13.827  1.00 35.68 ? 64  GLN A O   1 
ATOM   474  C  CB  . GLN A 1 64  ? -47.540 16.673  10.549  1.00 41.25 ? 64  GLN A CB  1 
ATOM   475  C  CG  . GLN A 1 64  ? -48.951 17.006  11.033  1.00 54.21 ? 64  GLN A CG  1 
ATOM   476  N  N   . LYS A 1 65  ? -46.476 14.350  12.551  1.00 37.15 ? 65  LYS A N   1 
ATOM   477  C  CA  . LYS A 1 65  ? -46.847 13.343  13.544  1.00 37.99 ? 65  LYS A CA  1 
ATOM   478  C  C   . LYS A 1 65  ? -46.127 13.518  14.884  1.00 37.17 ? 65  LYS A C   1 
ATOM   479  O  O   . LYS A 1 65  ? -46.612 12.989  15.877  1.00 39.29 ? 65  LYS A O   1 
ATOM   480  C  CB  . LYS A 1 65  ? -46.759 11.934  12.963  1.00 38.63 ? 65  LYS A CB  1 
ATOM   481  C  CG  . LYS A 1 65  ? -45.375 11.483  12.655  0.70 41.30 ? 65  LYS A CG  1 
ATOM   482  C  CD  . LYS A 1 65  ? -45.426 10.090  12.043  0.70 48.11 ? 65  LYS A CD  1 
ATOM   483  C  CE  . LYS A 1 65  ? -46.128 9.218   13.001  0.70 42.91 ? 65  LYS A CE  1 
ATOM   484  N  NZ  . LYS A 1 65  ? -45.688 7.837   12.827  0.70 45.94 ? 65  LYS A NZ  1 
ATOM   485  N  N   . PHE A 1 66  ? -45.004 14.254  14.949  1.00 34.23 ? 66  PHE A N   1 
ATOM   486  C  CA  . PHE A 1 66  ? -44.263 14.371  16.199  1.00 32.51 ? 66  PHE A CA  1 
ATOM   487  C  C   . PHE A 1 66  ? -44.293 15.804  16.727  1.00 34.08 ? 66  PHE A C   1 
ATOM   488  O  O   . PHE A 1 66  ? -43.592 16.098  17.679  1.00 36.24 ? 66  PHE A O   1 
ATOM   489  C  CB  . PHE A 1 66  ? -42.774 14.023  15.990  1.00 32.12 ? 66  PHE A CB  1 
ATOM   490  C  CG  . PHE A 1 66  ? -42.626 12.516  15.788  1.00 31.06 ? 66  PHE A CG  1 
ATOM   491  C  CD1 . PHE A 1 66  ? -42.625 11.644  16.881  1.00 32.22 ? 66  PHE A CD1 1 
ATOM   492  C  CD2 . PHE A 1 66  ? -42.498 11.978  14.519  1.00 29.62 ? 66  PHE A CD2 1 
ATOM   493  C  CE1 . PHE A 1 66  ? -42.509 10.270  16.690  1.00 30.05 ? 66  PHE A CE1 1 
ATOM   494  C  CE2 . PHE A 1 66  ? -42.375 10.603  14.327  1.00 30.96 ? 66  PHE A CE2 1 
ATOM   495  C  CZ  . PHE A 1 66  ? -42.373 9.747   15.422  1.00 33.80 ? 66  PHE A CZ  1 
ATOM   496  N  N   . LYS A 1 67  ? -45.143 16.693  16.172  1.00 33.43 ? 67  LYS A N   1 
ATOM   497  C  CA  . LYS A 1 67  ? -45.052 18.111  16.524  1.00 38.80 ? 67  LYS A CA  1 
ATOM   498  C  C   . LYS A 1 67  ? -45.365 18.337  18.003  1.00 40.16 ? 67  LYS A C   1 
ATOM   499  O  O   . LYS A 1 67  ? -44.768 19.207  18.620  1.00 49.52 ? 67  LYS A O   1 
ATOM   500  C  CB  . LYS A 1 67  ? -45.850 19.075  15.626  1.00 41.67 ? 67  LYS A CB  1 
ATOM   501  C  CG  . LYS A 1 67  ? -47.335 18.819  15.575  1.00 49.43 ? 67  LYS A CG  1 
ATOM   502  N  N   . ASP A 1 68  ? -46.277 17.549  18.583  1.00 39.66 ? 68  ASP A N   1 
ATOM   503  C  CA  . ASP A 1 68  ? -46.626 17.767  19.978  1.00 44.22 ? 68  ASP A CA  1 
ATOM   504  C  C   . ASP A 1 68  ? -45.678 16.976  20.890  1.00 41.77 ? 68  ASP A C   1 
ATOM   505  O  O   . ASP A 1 68  ? -45.390 17.403  21.990  1.00 46.11 ? 68  ASP A O   1 
ATOM   506  C  CB  . ASP A 1 68  ? -48.095 17.455  20.237  1.00 51.98 ? 68  ASP A CB  1 
ATOM   507  C  CG  . ASP A 1 68  ? -49.084 18.260  19.398  1.00 62.39 ? 68  ASP A CG  1 
ATOM   508  O  OD1 . ASP A 1 68  ? -48.934 19.504  19.344  1.00 58.00 ? 68  ASP A OD1 1 
ATOM   509  O  OD2 . ASP A 1 68  ? -49.970 17.636  18.765  1.00 64.54 ? 68  ASP A OD2 1 
ATOM   510  N  N   . LYS A 1 69  ? -45.131 15.879  20.382  1.00 35.16 ? 69  LYS A N   1 
ATOM   511  C  CA  . LYS A 1 69  ? -44.365 14.948  21.200  1.00 31.78 ? 69  LYS A CA  1 
ATOM   512  C  C   . LYS A 1 69  ? -42.929 15.435  21.414  1.00 31.95 ? 69  LYS A C   1 
ATOM   513  O  O   . LYS A 1 69  ? -42.393 15.204  22.504  1.00 35.00 ? 69  LYS A O   1 
ATOM   514  C  CB  . LYS A 1 69  ? -44.436 13.577  20.515  1.00 31.86 ? 69  LYS A CB  1 
ATOM   515  C  CG  . LYS A 1 69  ? -43.519 12.477  21.105  1.00 31.84 ? 69  LYS A CG  1 
ATOM   516  C  CD  . LYS A 1 69  ? -44.010 12.172  22.532  1.00 31.00 ? 69  LYS A CD  1 
ATOM   517  C  CE  . LYS A 1 69  ? -45.439 11.671  22.615  1.00 33.18 ? 69  LYS A CE  1 
ATOM   518  N  NZ  . LYS A 1 69  ? -45.826 11.242  23.982  1.00 34.18 ? 69  LYS A NZ  1 
ATOM   519  N  N   . ALA A 1 70  ? -42.291 16.028  20.381  1.00 30.16 ? 70  ALA A N   1 
ATOM   520  C  CA  . ALA A 1 70  ? -40.862 16.327  20.399  1.00 31.51 ? 70  ALA A CA  1 
ATOM   521  C  C   . ALA A 1 70  ? -40.612 17.824  20.418  1.00 32.52 ? 70  ALA A C   1 
ATOM   522  O  O   . ALA A 1 70  ? -41.312 18.573  19.738  1.00 35.39 ? 70  ALA A O   1 
ATOM   523  C  CB  . ALA A 1 70  ? -40.148 15.693  19.214  1.00 30.82 ? 70  ALA A CB  1 
ATOM   524  N  N   . THR A 1 71  ? -39.561 18.250  21.119  1.00 32.67 ? 71  THR A N   1 
ATOM   525  C  CA  . THR A 1 71  ? -39.069 19.626  21.017  1.00 33.25 ? 71  THR A CA  1 
ATOM   526  C  C   . THR A 1 71  ? -37.558 19.546  20.839  1.00 31.94 ? 71  THR A C   1 
ATOM   527  O  O   . THR A 1 71  ? -36.869 18.911  21.675  1.00 30.24 ? 71  THR A O   1 
ATOM   528  C  CB  . THR A 1 71  ? -39.393 20.466  22.264  1.00 33.82 ? 71  THR A CB  1 
ATOM   529  O  OG1 . THR A 1 71  ? -40.798 20.405  22.515  1.00 38.15 ? 71  THR A OG1 1 
ATOM   530  C  CG2 . THR A 1 71  ? -38.915 21.902  22.126  1.00 33.02 ? 71  THR A CG2 1 
ATOM   531  N  N   . LEU A 1 72  ? -37.051 20.193  19.774  1.00 31.75 ? 72  LEU A N   1 
ATOM   532  C  CA  . LEU A 1 72  ? -35.627 20.143  19.479  1.00 30.19 ? 72  LEU A CA  1 
ATOM   533  C  C   . LEU A 1 72  ? -34.965 21.457  19.886  1.00 31.63 ? 72  LEU A C   1 
ATOM   534  O  O   . LEU A 1 72  ? -35.478 22.529  19.540  1.00 34.15 ? 72  LEU A O   1 
ATOM   535  C  CB  . LEU A 1 72  ? -35.446 19.902  17.980  1.00 29.80 ? 72  LEU A CB  1 
ATOM   536  C  CG  . LEU A 1 72  ? -36.057 18.628  17.386  1.00 31.36 ? 72  LEU A CG  1 
ATOM   537  C  CD1 . LEU A 1 72  ? -35.608 18.465  15.916  1.00 30.79 ? 72  LEU A CD1 1 
ATOM   538  C  CD2 . LEU A 1 72  ? -35.677 17.396  18.261  1.00 31.11 ? 72  LEU A CD2 1 
ATOM   539  N  N   . THR A 1 73  ? -33.816 21.366  20.553  1.00 29.31 ? 73  THR A N   1 
ATOM   540  C  CA  . THR A 1 73  ? -33.025 22.550  20.878  1.00 33.10 ? 73  THR A CA  1 
ATOM   541  C  C   . THR A 1 73  ? -31.542 22.273  20.643  1.00 32.56 ? 73  THR A C   1 
ATOM   542  O  O   . THR A 1 73  ? -31.116 21.137  20.432  1.00 32.66 ? 73  THR A O   1 
ATOM   543  C  CB  . THR A 1 73  ? -33.286 23.030  22.319  1.00 37.15 ? 73  THR A CB  1 
ATOM   544  O  OG1 . THR A 1 73  ? -32.921 21.991  23.226  1.00 35.40 ? 73  THR A OG1 1 
ATOM   545  C  CG2 . THR A 1 73  ? -34.739 23.404  22.552  1.00 34.99 ? 73  THR A CG2 1 
ATOM   546  N  N   . ALA A 1 74  ? -30.752 23.344  20.684  1.00 31.41 ? 74  ALA A N   1 
ATOM   547  C  CA  . ALA A 1 74  ? -29.330 23.249  20.444  1.00 33.13 ? 74  ALA A CA  1 
ATOM   548  C  C   . ALA A 1 74  ? -28.622 24.226  21.372  1.00 40.49 ? 74  ALA A C   1 
ATOM   549  O  O   . ALA A 1 74  ? -29.095 25.359  21.523  1.00 38.61 ? 74  ALA A O   1 
ATOM   550  C  CB  . ALA A 1 74  ? -29.031 23.601  18.996  1.00 32.63 ? 74  ALA A CB  1 
ATOM   551  N  N   . ASP A 1 75  ? -27.494 23.772  21.933  1.00 34.87 ? 75  ASP A N   1 
ATOM   552  C  CA  . ASP A 1 75  ? -26.668 24.564  22.840  1.00 39.39 ? 75  ASP A CA  1 
ATOM   553  C  C   . ASP A 1 75  ? -25.281 24.709  22.238  1.00 34.55 ? 75  ASP A C   1 
ATOM   554  O  O   . ASP A 1 75  ? -24.413 23.825  22.346  1.00 35.17 ? 75  ASP A O   1 
ATOM   555  C  CB  . ASP A 1 75  ? -26.670 23.951  24.228  1.00 41.57 ? 75  ASP A CB  1 
ATOM   556  C  CG  . ASP A 1 75  ? -25.877 24.675  25.308  0.80 45.68 ? 75  ASP A CG  1 
ATOM   557  O  OD1 . ASP A 1 75  ? -25.192 25.638  24.984  0.80 43.86 ? 75  ASP A OD1 1 
ATOM   558  O  OD2 . ASP A 1 75  ? -25.933 24.230  26.468  0.80 52.56 ? 75  ASP A OD2 1 
ATOM   559  N  N   . LYS A 1 76  ? -25.100 25.829  21.541  1.00 38.89 ? 76  LYS A N   1 
ATOM   560  C  CA  . LYS A 1 76  ? -23.835 26.116  20.885  1.00 40.51 ? 76  LYS A CA  1 
ATOM   561  C  C   . LYS A 1 76  ? -22.660 26.102  21.863  1.00 39.59 ? 76  LYS A C   1 
ATOM   562  O  O   . LYS A 1 76  ? -21.579 25.680  21.487  1.00 44.27 ? 76  LYS A O   1 
ATOM   563  C  CB  . LYS A 1 76  ? -23.887 27.400  20.051  1.00 39.62 ? 76  LYS A CB  1 
ATOM   564  C  CG  . LYS A 1 76  ? -24.652 27.186  18.758  1.00 41.24 ? 76  LYS A CG  1 
ATOM   565  C  CD  . LYS A 1 76  ? -24.625 28.381  17.786  1.00 47.57 ? 76  LYS A CD  1 
ATOM   566  C  CE  . LYS A 1 76  ? -25.453 29.537  18.274  1.00 46.74 ? 76  LYS A CE  1 
ATOM   567  N  NZ  . LYS A 1 76  ? -25.339 30.593  17.263  1.00 48.72 ? 76  LYS A NZ  1 
ATOM   568  N  N   . SER A 1 77  ? -22.871 26.511  23.119  1.00 42.18 ? 77  SER A N   1 
ATOM   569  C  CA  . SER A 1 77  ? -21.781 26.585  24.084  1.00 41.73 ? 77  SER A CA  1 
ATOM   570  C  C   . SER A 1 77  ? -21.201 25.212  24.415  1.00 44.15 ? 77  SER A C   1 
ATOM   571  O  O   . SER A 1 77  ? -20.021 25.112  24.732  1.00 47.04 ? 77  SER A O   1 
ATOM   572  C  CB  . SER A 1 77  ? -22.155 27.364  25.352  1.00 48.21 ? 77  SER A CB  1 
ATOM   573  O  OG  . SER A 1 77  ? -23.212 26.728  26.052  1.00 49.31 ? 77  SER A OG  1 
ATOM   574  N  N   . SER A 1 78  ? -21.999 24.145  24.290  1.00 37.09 ? 78  SER A N   1 
ATOM   575  C  CA  . SER A 1 78  ? -21.512 22.802  24.572  1.00 36.49 ? 78  SER A CA  1 
ATOM   576  C  C   . SER A 1 78  ? -21.543 21.920  23.308  1.00 33.63 ? 78  SER A C   1 
ATOM   577  O  O   . SER A 1 78  ? -21.283 20.705  23.391  1.00 35.32 ? 78  SER A O   1 
ATOM   578  C  CB  . SER A 1 78  ? -22.362 22.194  25.650  1.00 37.33 ? 78  SER A CB  1 
ATOM   579  O  OG  . SER A 1 78  ? -23.692 22.061  25.154  1.00 37.55 ? 78  SER A OG  1 
ATOM   580  N  N   . SER A 1 79  ? -21.873 22.506  22.142  1.00 33.29 ? 79  SER A N   1 
ATOM   581  C  CA  . SER A 1 79  ? -21.925 21.719  20.908  1.00 31.86 ? 79  SER A CA  1 
ATOM   582  C  C   . SER A 1 79  ? -22.873 20.529  21.081  1.00 30.84 ? 79  SER A C   1 
ATOM   583  O  O   . SER A 1 79  ? -22.608 19.451  20.531  1.00 30.79 ? 79  SER A O   1 
ATOM   584  C  CB  . SER A 1 79  ? -20.563 21.240  20.445  1.00 35.90 ? 79  SER A CB  1 
ATOM   585  O  OG  . SER A 1 79  ? -19.655 22.321  20.229  1.00 38.54 ? 79  SER A OG  1 
ATOM   586  N  N   . THR A 1 80  ? -24.003 20.757  21.766  1.00 29.45 ? 80  THR A N   1 
ATOM   587  C  CA  . THR A 1 80  ? -24.901 19.636  22.066  1.00 29.43 ? 80  THR A CA  1 
ATOM   588  C  C   . THR A 1 80  ? -26.305 19.955  21.577  1.00 29.99 ? 80  THR A C   1 
ATOM   589  O  O   . THR A 1 80  ? -26.820 21.045  21.834  1.00 30.78 ? 80  THR A O   1 
ATOM   590  C  CB  . THR A 1 80  ? -24.905 19.360  23.579  1.00 32.47 ? 80  THR A CB  1 
ATOM   591  O  OG1 . THR A 1 80  ? -23.599 18.938  23.955  1.00 30.09 ? 80  THR A OG1 1 
ATOM   592  C  CG2 . THR A 1 80  ? -25.838 18.213  23.944  1.00 29.73 ? 80  THR A CG2 1 
ATOM   593  N  N   . ALA A 1 81  ? -26.942 18.984  20.910  1.00 27.72 ? 81  ALA A N   1 
ATOM   594  C  CA  . ALA A 1 81  ? -28.340 19.118  20.516  1.00 29.63 ? 81  ALA A CA  1 
ATOM   595  C  C   . ALA A 1 81  ? -29.164 18.288  21.483  1.00 27.95 ? 81  ALA A C   1 
ATOM   596  O  O   . ALA A 1 81  ? -28.676 17.276  21.991  1.00 30.08 ? 81  ALA A O   1 
ATOM   597  C  CB  . ALA A 1 81  ? -28.569 18.574  19.114  1.00 31.04 ? 81  ALA A CB  1 
ATOM   598  N  N   . TYR A 1 82  ? -30.413 18.672  21.661  1.00 27.14 ? 82  TYR A N   1 
ATOM   599  C  CA  . TYR A 1 82  ? -31.283 17.966  22.619  1.00 30.54 ? 82  TYR A CA  1 
ATOM   600  C  C   . TYR A 1 82  ? -32.654 17.764  22.062  1.00 29.57 ? 82  TYR A C   1 
ATOM   601  O  O   . TYR A 1 82  ? -33.150 18.617  21.318  1.00 29.10 ? 82  TYR A O   1 
ATOM   602  C  CB  . TYR A 1 82  ? -31.474 18.857  23.843  1.00 32.57 ? 82  TYR A CB  1 
ATOM   603  C  CG  . TYR A 1 82  ? -30.241 19.112  24.690  1.00 34.55 ? 82  TYR A CG  1 
ATOM   604  C  CD1 . TYR A 1 82  ? -29.817 18.181  25.624  1.00 32.81 ? 82  TYR A CD1 1 
ATOM   605  C  CD2 . TYR A 1 82  ? -29.511 20.285  24.559  1.00 33.80 ? 82  TYR A CD2 1 
ATOM   606  C  CE1 . TYR A 1 82  ? -28.697 18.405  26.401  1.00 37.77 ? 82  TYR A CE1 1 
ATOM   607  C  CE2 . TYR A 1 82  ? -28.386 20.519  25.329  1.00 37.06 ? 82  TYR A CE2 1 
ATOM   608  C  CZ  . TYR A 1 82  ? -27.983 19.578  26.259  1.00 40.71 ? 82  TYR A CZ  1 
ATOM   609  O  OH  . TYR A 1 82  ? -26.879 19.787  27.029  1.00 40.08 ? 82  TYR A OH  1 
ATOM   610  N  N   . MET A 1 83  ? -33.262 16.632  22.399  1.00 27.10 ? 83  MET A N   1 
ATOM   611  C  CA  . MET A 1 83  ? -34.648 16.428  22.052  1.00 28.43 ? 83  MET A CA  1 
ATOM   612  C  C   . MET A 1 83  ? -35.392 16.061  23.335  1.00 30.67 ? 83  MET A C   1 
ATOM   613  O  O   . MET A 1 83  ? -35.029 15.119  24.053  1.00 30.80 ? 83  MET A O   1 
ATOM   614  C  CB  . MET A 1 83  ? -34.815 15.254  21.058  1.00 28.15 ? 83  MET A CB  1 
ATOM   615  C  CG  . MET A 1 83  ? -36.269 14.925  20.804  1.00 26.68 ? 83  MET A CG  1 
ATOM   616  S  SD  . MET A 1 83  ? -36.546 13.786  19.431  1.00 31.40 ? 83  MET A SD  1 
ATOM   617  C  CE  . MET A 1 83  ? -35.837 12.280  20.147  1.00 32.57 ? 83  MET A CE  1 
ATOM   618  N  N   . GLN A 1 84  ? -36.461 16.809  23.592  1.00 30.13 ? 84  GLN A N   1 
ATOM   619  C  CA  . GLN A 1 84  ? -37.329 16.447  24.691  1.00 29.55 ? 84  GLN A CA  1 
ATOM   620  C  C   . GLN A 1 84  ? -38.536 15.698  24.147  1.00 31.28 ? 84  GLN A C   1 
ATOM   621  O  O   . GLN A 1 84  ? -39.163 16.141  23.172  1.00 31.00 ? 84  GLN A O   1 
ATOM   622  C  CB  . GLN A 1 84  ? -37.828 17.742  25.320  1.00 31.40 ? 84  GLN A CB  1 
ATOM   623  C  CG  . GLN A 1 84  ? -38.670 17.479  26.572  1.00 37.44 ? 84  GLN A CG  1 
ATOM   624  C  CD  . GLN A 1 84  ? -39.679 18.559  26.911  1.00 50.97 ? 84  GLN A CD  1 
ATOM   625  O  OE1 . GLN A 1 84  ? -40.546 18.927  26.108  1.00 55.43 ? 84  GLN A OE1 1 
ATOM   626  N  NE2 . GLN A 1 84  ? -39.592 19.058  28.134  1.00 51.29 ? 84  GLN A NE2 1 
ATOM   627  N  N   . LEU A 1 85  ? -38.877 14.581  24.806  1.00 29.97 ? 85  LEU A N   1 
ATOM   628  C  CA  . LEU A 1 85  ? -40.115 13.863  24.548  1.00 32.10 ? 85  LEU A CA  1 
ATOM   629  C  C   . LEU A 1 85  ? -41.044 14.096  25.729  1.00 32.84 ? 85  LEU A C   1 
ATOM   630  O  O   . LEU A 1 85  ? -40.646 13.847  26.855  1.00 35.05 ? 85  LEU A O   1 
ATOM   631  C  CB  . LEU A 1 85  ? -39.821 12.373  24.358  1.00 31.13 ? 85  LEU A CB  1 
ATOM   632  C  CG  . LEU A 1 85  ? -38.854 12.072  23.215  1.00 31.96 ? 85  LEU A CG  1 
ATOM   633  C  CD1 . LEU A 1 85  ? -38.583 10.566  23.392  1.00 29.24 ? 85  LEU A CD1 1 
ATOM   634  C  CD2 . LEU A 1 85  ? -39.442 12.332  21.795  1.00 31.03 ? 85  LEU A CD2 1 
ATOM   635  N  N   . SER A 1 86  ? -42.245 14.626  25.456  1.00 32.65 ? 86  SER A N   1 
ATOM   636  C  CA  . SER A 1 86  ? -43.141 15.003  26.539  1.00 34.47 ? 86  SER A CA  1 
ATOM   637  C  C   . SER A 1 86  ? -44.295 13.998  26.654  1.00 34.02 ? 86  SER A C   1 
ATOM   638  O  O   . SER A 1 86  ? -44.522 13.209  25.742  1.00 35.56 ? 86  SER A O   1 
ATOM   639  C  CB  . SER A 1 86  ? -43.605 16.415  26.307  1.00 36.33 ? 86  SER A CB  1 
ATOM   640  O  OG  . SER A 1 86  ? -44.416 16.430  25.147  1.00 39.88 ? 86  SER A OG  1 
ATOM   641  N  N   . ASN A 1 87  ? -44.969 13.963  27.818  1.00 34.65 ? 87  ASN A N   1 
ATOM   642  C  CA  . ASN A 1 87  ? -46.131 13.105  28.036  1.00 33.71 ? 87  ASN A CA  1 
ATOM   643  C  C   . ASN A 1 87  ? -45.875 11.670  27.601  1.00 33.06 ? 87  ASN A C   1 
ATOM   644  O  O   . ASN A 1 87  ? -46.626 11.127  26.803  1.00 33.69 ? 87  ASN A O   1 
ATOM   645  C  CB  . ASN A 1 87  ? -47.337 13.657  27.267  1.00 39.06 ? 87  ASN A CB  1 
ATOM   646  C  CG  . ASN A 1 87  ? -47.649 15.064  27.718  1.00 45.68 ? 87  ASN A CG  1 
ATOM   647  O  OD1 . ASN A 1 87  ? -47.826 15.274  28.919  1.00 47.85 ? 87  ASN A OD1 1 
ATOM   648  N  ND2 . ASN A 1 87  ? -47.637 16.034  26.810  1.00 43.85 ? 87  ASN A ND2 1 
ATOM   649  N  N   . LEU A 1 88  ? -44.851 11.024  28.178  1.00 33.07 ? 88  LEU A N   1 
ATOM   650  C  CA  . LEU A 1 88  ? -44.419 9.725   27.685  1.00 33.35 ? 88  LEU A CA  1 
ATOM   651  C  C   . LEU A 1 88  ? -45.534 8.691   27.826  1.00 35.10 ? 88  LEU A C   1 
ATOM   652  O  O   . LEU A 1 88  ? -46.242 8.655   28.839  1.00 36.84 ? 88  LEU A O   1 
ATOM   653  C  CB  . LEU A 1 88  ? -43.172 9.354   28.493  1.00 32.59 ? 88  LEU A CB  1 
ATOM   654  C  CG  . LEU A 1 88  ? -41.896 10.105  28.061  1.00 35.36 ? 88  LEU A CG  1 
ATOM   655  C  CD1 . LEU A 1 88  ? -40.755 9.933   29.076  1.00 34.18 ? 88  LEU A CD1 1 
ATOM   656  C  CD2 . LEU A 1 88  ? -41.412 9.691   26.664  1.00 33.01 ? 88  LEU A CD2 1 
ATOM   657  N  N   . THR A 1 89  ? -45.646 7.809   26.828  1.00 34.43 ? 89  THR A N   1 
ATOM   658  C  CA  . THR A 1 89  ? -46.546 6.661   26.904  1.00 35.09 ? 89  THR A CA  1 
ATOM   659  C  C   . THR A 1 89  ? -45.766 5.450   26.413  1.00 34.55 ? 89  THR A C   1 
ATOM   660  O  O   . THR A 1 89  ? -44.658 5.590   25.917  1.00 33.70 ? 89  THR A O   1 
ATOM   661  C  CB  . THR A 1 89  ? -47.803 6.840   26.045  1.00 36.54 ? 89  THR A CB  1 
ATOM   662  O  OG1 . THR A 1 89  ? -47.391 6.737   24.676  1.00 38.61 ? 89  THR A OG1 1 
ATOM   663  C  CG2 . THR A 1 89  ? -48.494 8.161   26.318  1.00 36.36 ? 89  THR A CG2 1 
ATOM   664  N  N   . SER A 1 90  ? -46.387 4.273   26.478  1.00 33.77 ? 90  SER A N   1 
ATOM   665  C  CA  . SER A 1 90  ? -45.750 3.048   26.028  1.00 34.57 ? 90  SER A CA  1 
ATOM   666  C  C   . SER A 1 90  ? -45.364 3.148   24.549  1.00 35.75 ? 90  SER A C   1 
ATOM   667  O  O   . SER A 1 90  ? -44.432 2.481   24.122  1.00 35.95 ? 90  SER A O   1 
ATOM   668  C  CB  . SER A 1 90  ? -46.659 1.849   26.273  1.00 38.21 ? 90  SER A CB  1 
ATOM   669  O  OG  . SER A 1 90  ? -46.920 1.761   27.670  1.00 42.89 ? 90  SER A OG  1 
ATOM   670  N  N   . GLU A 1 91  ? -46.108 3.947   23.770  1.00 32.24 ? 91  GLU A N   1 
ATOM   671  C  CA  . GLU A 1 91  ? -45.891 4.115   22.337  1.00 33.96 ? 91  GLU A CA  1 
ATOM   672  C  C   . GLU A 1 91  ? -44.584 4.862   22.046  1.00 32.02 ? 91  GLU A C   1 
ATOM   673  O  O   . GLU A 1 91  ? -44.142 4.843   20.882  1.00 32.07 ? 91  GLU A O   1 
ATOM   674  C  CB  . GLU A 1 91  ? -47.138 4.716   21.657  1.00 33.67 ? 91  GLU A CB  1 
ATOM   675  C  CG  . GLU A 1 91  ? -48.289 3.692   21.709  1.00 35.07 ? 91  GLU A CG  1 
ATOM   676  C  CD  . GLU A 1 91  ? -48.745 3.045   23.037  0.50 41.04 ? 91  GLU A CD  1 
ATOM   677  O  OE1 . GLU A 1 91  ? -49.250 3.820   23.897  0.50 40.32 ? 91  GLU A OE1 1 
ATOM   678  O  OE2 . GLU A 1 91  ? -48.610 1.788   23.277  0.50 40.62 ? 91  GLU A OE2 1 
ATOM   679  N  N   . ASP A 1 92  ? -43.951 5.474   23.075  1.00 30.61 ? 92  ASP A N   1 
ATOM   680  C  CA  . ASP A 1 92  ? -42.677 6.186   22.920  1.00 26.92 ? 92  ASP A CA  1 
ATOM   681  C  C   . ASP A 1 92  ? -41.459 5.283   23.221  1.00 29.53 ? 92  ASP A C   1 
ATOM   682  O  O   . ASP A 1 92  ? -40.304 5.678   22.934  1.00 28.68 ? 92  ASP A O   1 
ATOM   683  C  CB  . ASP A 1 92  ? -42.640 7.413   23.813  1.00 28.96 ? 92  ASP A CB  1 
ATOM   684  C  CG  . ASP A 1 92  ? -43.757 8.419   23.510  1.00 31.44 ? 92  ASP A CG  1 
ATOM   685  O  OD1 . ASP A 1 92  ? -43.988 8.696   22.280  1.00 32.46 ? 92  ASP A OD1 1 
ATOM   686  O  OD2 . ASP A 1 92  ? -44.392 8.935   24.501  1.00 33.39 ? 92  ASP A OD2 1 
ATOM   687  N  N   . SER A 1 93  ? -41.686 4.058   23.716  1.00 27.49 ? 93  SER A N   1 
ATOM   688  C  CA  . SER A 1 93  ? -40.584 3.115   23.935  1.00 28.81 ? 93  SER A CA  1 
ATOM   689  C  C   . SER A 1 93  ? -39.956 2.782   22.569  1.00 30.15 ? 93  SER A C   1 
ATOM   690  O  O   . SER A 1 93  ? -40.640 2.243   21.687  1.00 29.36 ? 93  SER A O   1 
ATOM   691  C  CB  . SER A 1 93  ? -41.073 1.848   24.634  1.00 28.44 ? 93  SER A CB  1 
ATOM   692  O  OG  . SER A 1 93  ? -41.441 2.152   25.974  1.00 29.00 ? 93  SER A OG  1 
ATOM   693  N  N   . ALA A 1 94  ? -38.642 3.035   22.414  1.00 27.20 ? 94  ALA A N   1 
ATOM   694  C  CA  . ALA A 1 94  ? -38.018 3.008   21.094  1.00 25.57 ? 94  ALA A CA  1 
ATOM   695  C  C   . ALA A 1 94  ? -36.554 3.394   21.233  1.00 24.97 ? 94  ALA A C   1 
ATOM   696  O  O   . ALA A 1 94  ? -36.130 3.817   22.316  1.00 26.76 ? 94  ALA A O   1 
ATOM   697  C  CB  . ALA A 1 94  ? -38.725 4.003   20.158  1.00 24.45 ? 94  ALA A CB  1 
ATOM   698  N  N   . VAL A 1 95  ? -35.759 3.218   20.169  1.00 25.17 ? 95  VAL A N   1 
ATOM   699  C  CA  . VAL A 1 95  ? -34.436 3.802   20.130  1.00 25.33 ? 95  VAL A CA  1 
ATOM   700  C  C   . VAL A 1 95  ? -34.490 5.107   19.323  1.00 25.34 ? 95  VAL A C   1 
ATOM   701  O  O   . VAL A 1 95  ? -35.195 5.162   18.295  1.00 23.97 ? 95  VAL A O   1 
ATOM   702  C  CB  . VAL A 1 95  ? -33.477 2.800   19.472  1.00 26.29 ? 95  VAL A CB  1 
ATOM   703  C  CG1 . VAL A 1 95  ? -32.068 3.393   19.504  1.00 25.54 ? 95  VAL A CG1 1 
ATOM   704  C  CG2 . VAL A 1 95  ? -33.441 1.479   20.287  1.00 24.94 ? 95  VAL A CG2 1 
ATOM   705  N  N   . TYR A 1 96  ? -33.816 6.170   19.802  1.00 23.32 ? 96  TYR A N   1 
ATOM   706  C  CA  . TYR A 1 96  ? -33.857 7.465   19.101  1.00 23.35 ? 96  TYR A CA  1 
ATOM   707  C  C   . TYR A 1 96  ? -32.421 7.818   18.733  1.00 23.76 ? 96  TYR A C   1 
ATOM   708  O  O   . TYR A 1 96  ? -31.555 7.871   19.620  1.00 25.48 ? 96  TYR A O   1 
ATOM   709  C  CB  . TYR A 1 96  ? -34.388 8.511   20.093  1.00 24.29 ? 96  TYR A CB  1 
ATOM   710  C  CG  . TYR A 1 96  ? -35.856 8.273   20.425  1.00 23.47 ? 96  TYR A CG  1 
ATOM   711  C  CD1 . TYR A 1 96  ? -36.245 7.435   21.461  1.00 27.36 ? 96  TYR A CD1 1 
ATOM   712  C  CD2 . TYR A 1 96  ? -36.837 8.899   19.667  1.00 22.52 ? 96  TYR A CD2 1 
ATOM   713  C  CE1 . TYR A 1 96  ? -37.591 7.180   21.725  1.00 27.57 ? 96  TYR A CE1 1 
ATOM   714  C  CE2 . TYR A 1 96  ? -38.180 8.679   19.939  1.00 24.10 ? 96  TYR A CE2 1 
ATOM   715  C  CZ  . TYR A 1 96  ? -38.552 7.811   20.947  1.00 26.81 ? 96  TYR A CZ  1 
ATOM   716  O  OH  . TYR A 1 96  ? -39.874 7.617   21.162  1.00 27.53 ? 96  TYR A OH  1 
ATOM   717  N  N   . TYR A 1 97  ? -32.206 8.141   17.434  1.00 24.46 ? 97  TYR A N   1 
ATOM   718  C  CA  . TYR A 1 97  ? -30.845 8.458   16.988  1.00 23.92 ? 97  TYR A CA  1 
ATOM   719  C  C   . TYR A 1 97  ? -30.823 9.934   16.623  1.00 23.40 ? 97  TYR A C   1 
ATOM   720  O  O   . TYR A 1 97  ? -31.830 10.462  16.128  1.00 25.56 ? 97  TYR A O   1 
ATOM   721  C  CB  . TYR A 1 97  ? -30.625 7.711   15.664  1.00 25.41 ? 97  TYR A CB  1 
ATOM   722  C  CG  . TYR A 1 97  ? -30.558 6.205   15.809  1.00 22.46 ? 97  TYR A CG  1 
ATOM   723  C  CD1 . TYR A 1 97  ? -29.349 5.580   16.181  1.00 23.55 ? 97  TYR A CD1 1 
ATOM   724  C  CD2 . TYR A 1 97  ? -31.699 5.417   15.699  1.00 24.65 ? 97  TYR A CD2 1 
ATOM   725  C  CE1 . TYR A 1 97  ? -29.318 4.200   16.416  1.00 24.85 ? 97  TYR A CE1 1 
ATOM   726  C  CE2 . TYR A 1 97  ? -31.651 4.036   15.913  1.00 24.70 ? 97  TYR A CE2 1 
ATOM   727  C  CZ  . TYR A 1 97  ? -30.467 3.443   16.314  1.00 25.11 ? 97  TYR A CZ  1 
ATOM   728  O  OH  . TYR A 1 97  ? -30.492 2.082   16.463  1.00 25.98 ? 97  TYR A OH  1 
ATOM   729  N  N   . CYS A 1 98  ? -29.665 10.560  16.831  1.00 25.13 ? 98  CYS A N   1 
ATOM   730  C  CA  . CYS A 1 98  ? -29.406 11.806  16.127  1.00 25.15 ? 98  CYS A CA  1 
ATOM   731  C  C   . CYS A 1 98  ? -28.461 11.550  14.960  1.00 25.92 ? 98  CYS A C   1 
ATOM   732  O  O   . CYS A 1 98  ? -27.639 10.643  14.991  1.00 23.17 ? 98  CYS A O   1 
ATOM   733  C  CB  . CYS A 1 98  ? -28.859 12.903  17.038  1.00 24.76 ? 98  CYS A CB  1 
ATOM   734  S  SG  . CYS A 1 98  ? -27.285 12.394  17.770  1.00 32.42 ? 98  CYS A SG  1 
ATOM   735  N  N   . ALA A 1 99  ? -28.610 12.306  13.855  1.00 23.68 ? 99  ALA A N   1 
ATOM   736  C  CA  . ALA A 1 99  ? -27.816 11.993  12.675  1.00 23.59 ? 99  ALA A CA  1 
ATOM   737  C  C   . ALA A 1 99  ? -27.715 13.186  11.703  1.00 25.80 ? 99  ALA A C   1 
ATOM   738  O  O   . ALA A 1 99  ? -28.627 14.026  11.630  1.00 26.73 ? 99  ALA A O   1 
ATOM   739  C  CB  . ALA A 1 99  ? -28.472 10.850  11.904  1.00 23.18 ? 99  ALA A CB  1 
ATOM   740  N  N   . ARG A 1 100 ? -26.619 13.273  10.956  1.00 23.96 ? 100 ARG A N   1 
ATOM   741  C  CA  . ARG A 1 100 ? -26.638 14.023  9.689   1.00 24.50 ? 100 ARG A CA  1 
ATOM   742  C  C   . ARG A 1 100 ? -27.141 13.063  8.627   1.00 24.85 ? 100 ARG A C   1 
ATOM   743  O  O   . ARG A 1 100 ? -26.509 12.010  8.372   1.00 24.36 ? 100 ARG A O   1 
ATOM   744  C  CB  . ARG A 1 100 ? -25.243 14.571  9.373   1.00 24.37 ? 100 ARG A CB  1 
ATOM   745  C  CG  . ARG A 1 100 ? -24.848 15.533  10.482  1.00 26.24 ? 100 ARG A CG  1 
ATOM   746  C  CD  . ARG A 1 100 ? -23.557 16.280  10.118  1.00 26.02 ? 100 ARG A CD  1 
ATOM   747  N  NE  . ARG A 1 100 ? -22.563 15.403  9.488   1.00 28.45 ? 100 ARG A NE  1 
ATOM   748  C  CZ  . ARG A 1 100 ? -21.237 15.514  9.605   1.00 34.81 ? 100 ARG A CZ  1 
ATOM   749  N  NH1 . ARG A 1 100 ? -20.712 16.497  10.343  1.00 41.75 ? 100 ARG A NH1 1 
ATOM   750  N  NH2 . ARG A 1 100 ? -20.413 14.715  8.942   1.00 32.24 ? 100 ARG A NH2 1 
ATOM   751  N  N   . LEU A 1 101 ? -28.263 13.445  7.994   1.00 23.48 ? 101 LEU A N   1 
ATOM   752  C  CA  . LEU A 1 101 ? -28.948 12.511  7.081   1.00 26.80 ? 101 LEU A CA  1 
ATOM   753  C  C   . LEU A 1 101 ? -28.614 12.727  5.605   1.00 27.44 ? 101 LEU A C   1 
ATOM   754  O  O   . LEU A 1 101 ? -28.705 11.794  4.787   1.00 27.46 ? 101 LEU A O   1 
ATOM   755  C  CB  . LEU A 1 101 ? -30.465 12.369  7.274   1.00 27.01 ? 101 LEU A CB  1 
ATOM   756  C  CG  . LEU A 1 101 ? -30.892 11.720  8.593   1.00 26.91 ? 101 LEU A CG  1 
ATOM   757  C  CD1 . LEU A 1 101 ? -32.437 11.762  8.611   1.00 24.87 ? 101 LEU A CD1 1 
ATOM   758  C  CD2 . LEU A 1 101 ? -30.324 10.287  8.690   1.00 28.60 ? 101 LEU A CD2 1 
ATOM   759  N  N   . ASP A 1 102 ? -28.139 13.916  5.222   1.00 28.58 ? 102 ASP A N   1 
ATOM   760  C  CA  . ASP A 1 102 ? -27.836 14.033  3.797   1.00 29.37 ? 102 ASP A CA  1 
ATOM   761  C  C   . ASP A 1 102 ? -26.693 13.069  3.462   1.00 28.96 ? 102 ASP A C   1 
ATOM   762  O  O   . ASP A 1 102 ? -25.736 12.971  4.238   1.00 29.25 ? 102 ASP A O   1 
ATOM   763  C  CB  . ASP A 1 102 ? -27.409 15.478  3.521   1.00 33.00 ? 102 ASP A CB  1 
ATOM   764  C  CG  . ASP A 1 102 ? -28.548 16.484  3.639   1.00 38.14 ? 102 ASP A CG  1 
ATOM   765  O  OD1 . ASP A 1 102 ? -29.711 16.105  3.325   1.00 41.14 ? 102 ASP A OD1 1 
ATOM   766  O  OD2 . ASP A 1 102 ? -28.261 17.611  4.035   1.00 49.11 ? 102 ASP A OD2 1 
ATOM   767  N  N   . TRP A 1 103 ? -26.768 12.354  2.338   1.00 27.19 ? 103 TRP A N   1 
ATOM   768  C  CA  . TRP A 1 103 ? -25.851 11.240  2.146   1.00 26.75 ? 103 TRP A CA  1 
ATOM   769  C  C   . TRP A 1 103 ? -24.394 11.713  2.206   1.00 27.23 ? 103 TRP A C   1 
ATOM   770  O  O   . TRP A 1 103 ? -23.501 11.006  2.713   1.00 27.70 ? 103 TRP A O   1 
ATOM   771  C  CB  . TRP A 1 103 ? -26.147 10.466  0.839   1.00 25.54 ? 103 TRP A CB  1 
ATOM   772  C  CG  . TRP A 1 103 ? -26.003 11.230  -0.457  1.00 28.61 ? 103 TRP A CG  1 
ATOM   773  C  CD1 . TRP A 1 103 ? -27.025 11.766  -1.211  1.00 30.85 ? 103 TRP A CD1 1 
ATOM   774  C  CD2 . TRP A 1 103 ? -24.778 11.486  -1.187  1.00 27.22 ? 103 TRP A CD2 1 
ATOM   775  N  NE1 . TRP A 1 103 ? -26.508 12.342  -2.343  1.00 33.88 ? 103 TRP A NE1 1 
ATOM   776  C  CE2 . TRP A 1 103 ? -25.141 12.191  -2.349  1.00 31.61 ? 103 TRP A CE2 1 
ATOM   777  C  CE3 . TRP A 1 103 ? -23.438 11.132  -0.998  1.00 27.46 ? 103 TRP A CE3 1 
ATOM   778  C  CZ2 . TRP A 1 103 ? -24.186 12.598  -3.296  1.00 34.71 ? 103 TRP A CZ2 1 
ATOM   779  C  CZ3 . TRP A 1 103 ? -22.490 11.547  -1.915  1.00 28.13 ? 103 TRP A CZ3 1 
ATOM   780  C  CH2 . TRP A 1 103 ? -22.865 12.275  -3.046  1.00 32.09 ? 103 TRP A CH2 1 
ATOM   781  N  N   . TYR A 1 104 ? -24.125 12.886  1.621   1.00 25.42 ? 104 TYR A N   1 
ATOM   782  C  CA  . TYR A 1 104 ? -22.741 13.333  1.552   1.00 25.12 ? 104 TYR A CA  1 
ATOM   783  C  C   . TYR A 1 104 ? -22.173 13.740  2.919   1.00 26.05 ? 104 TYR A C   1 
ATOM   784  O  O   . TYR A 1 104 ? -20.949 13.865  3.041   1.00 28.89 ? 104 TYR A O   1 
ATOM   785  C  CB  . TYR A 1 104 ? -22.606 14.428  0.462   1.00 28.42 ? 104 TYR A CB  1 
ATOM   786  C  CG  . TYR A 1 104 ? -23.826 15.346  0.405   1.00 25.30 ? 104 TYR A CG  1 
ATOM   787  C  CD1 . TYR A 1 104 ? -23.948 16.370  1.339   1.00 27.51 ? 104 TYR A CD1 1 
ATOM   788  C  CD2 . TYR A 1 104 ? -24.810 15.195  -0.559  1.00 26.42 ? 104 TYR A CD2 1 
ATOM   789  C  CE1 . TYR A 1 104 ? -25.053 17.208  1.326   1.00 28.86 ? 104 TYR A CE1 1 
ATOM   790  C  CE2 . TYR A 1 104 ? -25.910 16.050  -0.597  1.00 29.72 ? 104 TYR A CE2 1 
ATOM   791  C  CZ  . TYR A 1 104 ? -26.017 17.056  0.351   1.00 29.20 ? 104 TYR A CZ  1 
ATOM   792  O  OH  . TYR A 1 104 ? -27.030 17.980  0.339   1.00 38.14 ? 104 TYR A OH  1 
ATOM   793  N  N   . PHE A 1 105 ? -23.014 13.974  3.938   1.00 25.25 ? 105 PHE A N   1 
ATOM   794  C  CA  . PHE A 1 105 ? -22.509 14.248  5.273   1.00 24.73 ? 105 PHE A CA  1 
ATOM   795  C  C   . PHE A 1 105 ? -22.843 13.108  6.267   1.00 25.61 ? 105 PHE A C   1 
ATOM   796  O  O   . PHE A 1 105 ? -22.757 13.321  7.446   1.00 24.72 ? 105 PHE A O   1 
ATOM   797  C  CB  . PHE A 1 105 ? -22.976 15.571  5.895   1.00 27.31 ? 105 PHE A CB  1 
ATOM   798  C  CG  . PHE A 1 105 ? -22.719 16.793  4.986   1.00 27.29 ? 105 PHE A CG  1 
ATOM   799  C  CD1 . PHE A 1 105 ? -21.534 16.890  4.263   1.00 28.20 ? 105 PHE A CD1 1 
ATOM   800  C  CD2 . PHE A 1 105 ? -23.696 17.778  4.807   1.00 28.53 ? 105 PHE A CD2 1 
ATOM   801  C  CE1 . PHE A 1 105 ? -21.270 18.003  3.446   1.00 27.46 ? 105 PHE A CE1 1 
ATOM   802  C  CE2 . PHE A 1 105 ? -23.425 18.918  3.996   1.00 27.12 ? 105 PHE A CE2 1 
ATOM   803  C  CZ  . PHE A 1 105 ? -22.258 18.965  3.265   1.00 27.91 ? 105 PHE A CZ  1 
ATOM   804  N  N   . ASP A 1 106 ? -23.192 11.909  5.770   1.00 25.31 ? 106 ASP A N   1 
ATOM   805  C  CA  . ASP A 1 106 ? -23.810 10.887  6.629   1.00 24.57 ? 106 ASP A CA  1 
ATOM   806  C  C   . ASP A 1 106 ? -23.002 10.660  7.907   1.00 26.41 ? 106 ASP A C   1 
ATOM   807  O  O   . ASP A 1 106 ? -21.790 10.404  7.872   1.00 25.97 ? 106 ASP A O   1 
ATOM   808  C  CB  . ASP A 1 106 ? -23.766 9.564   5.882   1.00 22.90 ? 106 ASP A CB  1 
ATOM   809  C  CG  . ASP A 1 106 ? -24.422 8.384   6.633   1.00 23.39 ? 106 ASP A CG  1 
ATOM   810  O  OD1 . ASP A 1 106 ? -25.635 8.466   6.825   1.00 27.56 ? 106 ASP A OD1 1 
ATOM   811  O  OD2 . ASP A 1 106 ? -23.672 7.426   7.053   1.00 25.87 ? 106 ASP A OD2 1 
ATOM   812  N  N   . LEU A 1 107 ? -23.704 10.704  9.036   1.00 23.03 ? 107 LEU A N   1 
ATOM   813  C  CA  . LEU A 1 107 ? -23.108 10.517  10.377  1.00 23.24 ? 107 LEU A CA  1 
ATOM   814  C  C   . LEU A 1 107 ? -24.238 10.206  11.337  1.00 25.65 ? 107 LEU A C   1 
ATOM   815  O  O   . LEU A 1 107 ? -25.226 10.958  11.405  1.00 24.55 ? 107 LEU A O   1 
ATOM   816  C  CB  . LEU A 1 107 ? -22.369 11.805  10.797  1.00 24.01 ? 107 LEU A CB  1 
ATOM   817  C  CG  . LEU A 1 107 ? -21.664 11.770  12.171  1.00 25.69 ? 107 LEU A CG  1 
ATOM   818  C  CD1 . LEU A 1 107 ? -20.520 10.765  12.135  1.00 28.73 ? 107 LEU A CD1 1 
ATOM   819  C  CD2 . LEU A 1 107 ? -21.179 13.177  12.462  1.00 28.61 ? 107 LEU A CD2 1 
ATOM   820  N  N   . TRP A 1 108 ? -24.067 9.127   12.142  1.00 25.05 ? 108 TRP A N   1 
ATOM   821  C  CA  . TRP A 1 108 ? -25.123 8.749   13.091  1.00 25.46 ? 108 TRP A CA  1 
ATOM   822  C  C   . TRP A 1 108 ? -24.567 8.596   14.504  1.00 25.11 ? 108 TRP A C   1 
ATOM   823  O  O   . TRP A 1 108 ? -23.435 8.105   14.673  1.00 25.79 ? 108 TRP A O   1 
ATOM   824  C  CB  . TRP A 1 108 ? -25.689 7.381   12.668  1.00 24.66 ? 108 TRP A CB  1 
ATOM   825  C  CG  . TRP A 1 108 ? -26.442 7.387   11.366  1.00 26.33 ? 108 TRP A CG  1 
ATOM   826  C  CD1 . TRP A 1 108 ? -25.959 7.550   10.085  1.00 22.61 ? 108 TRP A CD1 1 
ATOM   827  C  CD2 . TRP A 1 108 ? -27.868 7.223   11.245  1.00 25.34 ? 108 TRP A CD2 1 
ATOM   828  N  NE1 . TRP A 1 108 ? -27.003 7.477   9.189   1.00 22.63 ? 108 TRP A NE1 1 
ATOM   829  C  CE2 . TRP A 1 108 ? -28.169 7.266   9.868   1.00 24.57 ? 108 TRP A CE2 1 
ATOM   830  C  CE3 . TRP A 1 108 ? -28.919 6.997   12.160  1.00 25.17 ? 108 TRP A CE3 1 
ATOM   831  C  CZ2 . TRP A 1 108 ? -29.470 7.121   9.366   1.00 24.73 ? 108 TRP A CZ2 1 
ATOM   832  C  CZ3 . TRP A 1 108 ? -30.189 6.851   11.659  1.00 25.66 ? 108 TRP A CZ3 1 
ATOM   833  C  CH2 . TRP A 1 108 ? -30.465 6.864   10.293  1.00 25.56 ? 108 TRP A CH2 1 
ATOM   834  N  N   . GLY A 1 109 ? -25.369 9.023   15.501  1.00 24.33 ? 109 GLY A N   1 
ATOM   835  C  CA  . GLY A 1 109 ? -25.126 8.607   16.875  1.00 23.48 ? 109 GLY A CA  1 
ATOM   836  C  C   . GLY A 1 109 ? -25.488 7.139   17.086  1.00 24.68 ? 109 GLY A C   1 
ATOM   837  O  O   . GLY A 1 109 ? -26.078 6.509   16.198  1.00 25.66 ? 109 GLY A O   1 
ATOM   838  N  N   . ALA A 1 110 ? -25.078 6.579   18.278  1.00 23.96 ? 110 ALA A N   1 
ATOM   839  C  CA  . ALA A 1 110 ? -25.389 5.160   18.495  1.00 25.73 ? 110 ALA A CA  1 
ATOM   840  C  C   . ALA A 1 110 ? -26.829 4.930   18.950  1.00 24.50 ? 110 ALA A C   1 
ATOM   841  O  O   . ALA A 1 110 ? -27.316 3.756   19.039  1.00 25.64 ? 110 ALA A O   1 
ATOM   842  C  CB  . ALA A 1 110 ? -24.379 4.651   19.489  1.00 26.15 ? 110 ALA A CB  1 
ATOM   843  N  N   . GLY A 1 111 ? -27.536 6.011   19.292  1.00 23.76 ? 111 GLY A N   1 
ATOM   844  C  CA  . GLY A 1 111 ? -28.938 5.882   19.646  1.00 23.10 ? 111 GLY A CA  1 
ATOM   845  C  C   . GLY A 1 111 ? -29.135 5.737   21.175  1.00 24.55 ? 111 GLY A C   1 
ATOM   846  O  O   . GLY A 1 111 ? -28.285 5.128   21.841  1.00 28.30 ? 111 GLY A O   1 
ATOM   847  N  N   . THR A 1 112 ? -30.218 6.349   21.710  1.00 25.17 ? 112 THR A N   1 
ATOM   848  C  CA  . THR A 1 112 ? -30.611 6.258   23.116  1.00 24.71 ? 112 THR A CA  1 
ATOM   849  C  C   . THR A 1 112 ? -31.869 5.401   23.161  1.00 25.16 ? 112 THR A C   1 
ATOM   850  O  O   . THR A 1 112 ? -32.860 5.756   22.530  1.00 26.59 ? 112 THR A O   1 
ATOM   851  C  CB  . THR A 1 112 ? -30.839 7.625   23.767  1.00 27.70 ? 112 THR A CB  1 
ATOM   852  O  OG1 . THR A 1 112 ? -29.592 8.326   23.724  1.00 27.21 ? 112 THR A OG1 1 
ATOM   853  C  CG2 . THR A 1 112 ? -31.336 7.478   25.208  1.00 27.44 ? 112 THR A CG2 1 
ATOM   854  N  N   . THR A 1 113 ? -31.811 4.278   23.903  1.00 24.55 ? 113 THR A N   1 
ATOM   855  C  CA  . THR A 1 113 ? -33.012 3.478   24.138  1.00 24.94 ? 113 THR A CA  1 
ATOM   856  C  C   . THR A 1 113 ? -33.839 4.147   25.228  1.00 26.99 ? 113 THR A C   1 
ATOM   857  O  O   . THR A 1 113 ? -33.344 4.295   26.341  1.00 29.81 ? 113 THR A O   1 
ATOM   858  C  CB  . THR A 1 113 ? -32.594 2.076   24.582  1.00 27.24 ? 113 THR A CB  1 
ATOM   859  O  OG1 . THR A 1 113 ? -31.941 1.408   23.504  1.00 25.83 ? 113 THR A OG1 1 
ATOM   860  C  CG2 . THR A 1 113 ? -33.807 1.207   24.931  1.00 26.71 ? 113 THR A CG2 1 
ATOM   861  N  N   . VAL A 1 114 ? -35.087 4.522   24.915  1.00 26.42 ? 114 VAL A N   1 
ATOM   862  C  CA  . VAL A 1 114 ? -35.961 5.102   25.921  1.00 26.86 ? 114 VAL A CA  1 
ATOM   863  C  C   . VAL A 1 114 ? -36.983 4.016   26.228  1.00 27.90 ? 114 VAL A C   1 
ATOM   864  O  O   . VAL A 1 114 ? -37.697 3.556   25.308  1.00 27.83 ? 114 VAL A O   1 
ATOM   865  C  CB  . VAL A 1 114 ? -36.699 6.331   25.356  1.00 28.10 ? 114 VAL A CB  1 
ATOM   866  C  CG1 . VAL A 1 114 ? -37.759 6.841   26.325  1.00 30.20 ? 114 VAL A CG1 1 
ATOM   867  C  CG2 . VAL A 1 114 ? -35.706 7.436   25.002  1.00 27.20 ? 114 VAL A CG2 1 
ATOM   868  N  N   . THR A 1 115 ? -37.053 3.631   27.521  1.00 26.16 ? 115 THR A N   1 
ATOM   869  C  CA  . THR A 1 115 ? -37.927 2.515   27.909  1.00 26.81 ? 115 THR A CA  1 
ATOM   870  C  C   . THR A 1 115 ? -38.982 3.073   28.862  1.00 29.43 ? 115 THR A C   1 
ATOM   871  O  O   . THR A 1 115 ? -38.633 3.456   29.985  1.00 28.25 ? 115 THR A O   1 
ATOM   872  C  CB  . THR A 1 115 ? -37.113 1.437   28.629  1.00 27.77 ? 115 THR A CB  1 
ATOM   873  O  OG1 . THR A 1 115 ? -36.133 0.966   27.705  1.00 27.84 ? 115 THR A OG1 1 
ATOM   874  C  CG2 . THR A 1 115 ? -37.974 0.223   28.959  1.00 27.21 ? 115 THR A CG2 1 
ATOM   875  N  N   . VAL A 1 116 ? -40.225 3.231   28.370  1.00 29.01 ? 116 VAL A N   1 
ATOM   876  C  CA  . VAL A 1 116 ? -41.270 3.772   29.210  1.00 29.21 ? 116 VAL A CA  1 
ATOM   877  C  C   . VAL A 1 116 ? -41.848 2.566   29.959  1.00 31.79 ? 116 VAL A C   1 
ATOM   878  O  O   . VAL A 1 116 ? -42.409 1.670   29.316  1.00 31.74 ? 116 VAL A O   1 
ATOM   879  C  CB  . VAL A 1 116 ? -42.339 4.466   28.372  1.00 32.47 ? 116 VAL A CB  1 
ATOM   880  C  CG1 . VAL A 1 116 ? -43.428 5.022   29.290  1.00 35.20 ? 116 VAL A CG1 1 
ATOM   881  C  CG2 . VAL A 1 116 ? -41.704 5.591   27.551  1.00 30.89 ? 116 VAL A CG2 1 
ATOM   882  N  N   . SER A 1 117 ? -41.676 2.570   31.296  1.00 30.66 ? 117 SER A N   1 
ATOM   883  C  CA  . SER A 1 117 ? -41.773 1.361   32.112  1.00 30.90 ? 117 SER A CA  1 
ATOM   884  C  C   . SER A 1 117 ? -42.787 1.581   33.225  1.00 35.35 ? 117 SER A C   1 
ATOM   885  O  O   . SER A 1 117 ? -42.645 2.518   34.030  1.00 34.96 ? 117 SER A O   1 
ATOM   886  C  CB  . SER A 1 117 ? -40.394 1.033   32.642  1.00 28.81 ? 117 SER A CB  1 
ATOM   887  O  OG  . SER A 1 117 ? -40.364 -0.039  33.580  1.00 30.67 ? 117 SER A OG  1 
ATOM   888  N  N   . ALA A 1 118 ? -43.825 0.734   33.235  1.00 35.04 ? 118 ALA A N   1 
ATOM   889  C  CA  . ALA A 1 118 ? -44.779 0.706   34.333  1.00 36.52 ? 118 ALA A CA  1 
ATOM   890  C  C   . ALA A 1 118 ? -45.426 -0.672  34.360  1.00 41.98 ? 118 ALA A C   1 
ATOM   891  O  O   . ALA A 1 118 ? -46.165 -1.012  33.443  1.00 39.75 ? 118 ALA A O   1 
ATOM   892  C  CB  . ALA A 1 118 ? -45.814 1.809   34.135  1.00 38.67 ? 118 ALA A CB  1 
ATOM   893  N  N   . ALA A 1 119 ? -45.152 -1.454  35.416  1.00 45.47 ? 119 ALA A N   1 
ATOM   894  C  CA  . ALA A 1 119 ? -45.541 -2.865  35.432  1.00 51.01 ? 119 ALA A CA  1 
ATOM   895  C  C   . ALA A 1 119 ? -47.051 -3.056  35.634  1.00 56.76 ? 119 ALA A C   1 
ATOM   896  O  O   . ALA A 1 119 ? -47.566 -4.152  35.381  1.00 56.08 ? 119 ALA A O   1 
ATOM   897  C  CB  . ALA A 1 119 ? -44.746 -3.638  36.480  1.00 52.87 ? 119 ALA A CB  1 
ATOM   898  N  N   . GLY A 1 120 ? -47.745 -2.000  36.099  1.00 57.30 ? 120 GLY A N   1 
ATOM   899  C  CA  . GLY A 1 120 ? -49.169 -2.069  36.404  1.00 78.78 ? 120 GLY A CA  1 
ATOM   900  C  C   . GLY A 1 120 ? -49.430 -2.607  37.811  1.00 83.21 ? 120 GLY A C   1 
ATOM   901  O  O   . GLY A 1 120 ? -49.701 -3.831  37.935  1.00 76.14 ? 120 GLY A O   1 
ATOM   902  N  N   . SER A 1 134 ? -50.626 11.305  2.473   1.00 50.34 ? 134 SER A N   1 
ATOM   903  C  CA  . SER A 1 134 ? -49.772 11.755  1.346   1.00 48.41 ? 134 SER A CA  1 
ATOM   904  C  C   . SER A 1 134 ? -48.278 11.618  1.656   1.00 42.39 ? 134 SER A C   1 
ATOM   905  O  O   . SER A 1 134 ? -47.457 11.938  0.805   1.00 42.70 ? 134 SER A O   1 
ATOM   906  C  CB  . SER A 1 134 ? -50.094 13.171  0.911   1.00 53.68 ? 134 SER A CB  1 
ATOM   907  O  OG  . SER A 1 134 ? -49.803 14.097  1.950   1.00 55.66 ? 134 SER A OG  1 
ATOM   908  N  N   . ASP A 1 135 ? -47.896 11.153  2.846   1.00 42.30 ? 135 ASP A N   1 
ATOM   909  C  CA  . ASP A 1 135 ? -46.482 10.847  3.034   1.00 40.85 ? 135 ASP A CA  1 
ATOM   910  C  C   . ASP A 1 135 ? -46.112 9.696   2.114   1.00 36.99 ? 135 ASP A C   1 
ATOM   911  O  O   . ASP A 1 135 ? -46.943 8.825   1.875   1.00 37.13 ? 135 ASP A O   1 
ATOM   912  C  CB  . ASP A 1 135 ? -46.149 10.446  4.461   1.00 41.07 ? 135 ASP A CB  1 
ATOM   913  C  CG  . ASP A 1 135 ? -46.330 11.562  5.479   1.00 50.18 ? 135 ASP A CG  1 
ATOM   914  O  OD1 . ASP A 1 135 ? -46.608 12.706  5.043   1.00 50.36 ? 135 ASP A OD1 1 
ATOM   915  O  OD2 . ASP A 1 135 ? -46.224 11.277  6.696   1.00 48.99 ? 135 ASP A OD2 1 
ATOM   916  N  N   . ILE A 1 136 ? -44.859 9.651   1.645   1.00 30.89 ? 136 ILE A N   1 
ATOM   917  C  CA  . ILE A 1 136 ? -44.517 8.525   0.788   1.00 29.45 ? 136 ILE A CA  1 
ATOM   918  C  C   . ILE A 1 136 ? -44.284 7.304   1.664   1.00 33.30 ? 136 ILE A C   1 
ATOM   919  O  O   . ILE A 1 136 ? -43.548 7.407   2.640   1.00 33.06 ? 136 ILE A O   1 
ATOM   920  C  CB  . ILE A 1 136 ? -43.267 8.887   -0.028  1.00 29.58 ? 136 ILE A CB  1 
ATOM   921  C  CG1 . ILE A 1 136 ? -43.595 10.081  -0.930  1.00 32.76 ? 136 ILE A CG1 1 
ATOM   922  C  CG2 . ILE A 1 136 ? -42.799 7.685   -0.851  1.00 32.84 ? 136 ILE A CG2 1 
ATOM   923  C  CD1 . ILE A 1 136 ? -42.481 10.475  -1.861  1.00 35.23 ? 136 ILE A CD1 1 
ATOM   924  N  N   . VAL A 1 137 ? -44.946 6.175   1.349   1.00 30.73 ? 137 VAL A N   1 
ATOM   925  C  CA  . VAL A 1 137 ? -44.747 4.946   2.090   1.00 30.78 ? 137 VAL A CA  1 
ATOM   926  C  C   . VAL A 1 137 ? -43.750 4.085   1.320   1.00 31.48 ? 137 VAL A C   1 
ATOM   927  O  O   . VAL A 1 137 ? -43.902 3.887   0.124   1.00 31.28 ? 137 VAL A O   1 
ATOM   928  C  CB  . VAL A 1 137 ? -46.092 4.201   2.256   1.00 32.00 ? 137 VAL A CB  1 
ATOM   929  C  CG1 . VAL A 1 137 ? -45.931 2.847   2.969   1.00 31.77 ? 137 VAL A CG1 1 
ATOM   930  C  CG2 . VAL A 1 137 ? -47.124 5.099   2.932   1.00 36.58 ? 137 VAL A CG2 1 
ATOM   931  N  N   . LEU A 1 138 ? -42.750 3.538   2.032   1.00 28.43 ? 138 LEU A N   1 
ATOM   932  C  CA  . LEU A 1 138 ? -41.798 2.597   1.476   1.00 28.31 ? 138 LEU A CA  1 
ATOM   933  C  C   . LEU A 1 138 ? -42.049 1.211   2.067   1.00 28.27 ? 138 LEU A C   1 
ATOM   934  O  O   . LEU A 1 138 ? -42.051 1.049   3.312   1.00 30.19 ? 138 LEU A O   1 
ATOM   935  C  CB  . LEU A 1 138 ? -40.378 3.035   1.830   1.00 28.19 ? 138 LEU A CB  1 
ATOM   936  C  CG  . LEU A 1 138 ? -39.961 4.422   1.348   1.00 30.31 ? 138 LEU A CG  1 
ATOM   937  C  CD1 . LEU A 1 138 ? -38.514 4.723   1.691   1.00 31.07 ? 138 LEU A CD1 1 
ATOM   938  C  CD2 . LEU A 1 138 ? -40.175 4.616   -0.115  1.00 31.00 ? 138 LEU A CD2 1 
ATOM   939  N  N   . THR A 1 139 ? -42.237 0.213   1.163   1.00 27.49 ? 139 THR A N   1 
ATOM   940  C  CA  . THR A 1 139 ? -42.469 -1.169  1.594   1.00 27.31 ? 139 THR A CA  1 
ATOM   941  C  C   . THR A 1 139 ? -41.270 -2.011  1.178   1.00 25.74 ? 139 THR A C   1 
ATOM   942  O  O   . THR A 1 139 ? -40.941 -2.056  -0.020  1.00 30.04 ? 139 THR A O   1 
ATOM   943  C  CB  . THR A 1 139 ? -43.734 -1.726  0.923   1.00 30.79 ? 139 THR A CB  1 
ATOM   944  O  OG1 . THR A 1 139 ? -44.752 -0.789  1.255   1.00 32.05 ? 139 THR A OG1 1 
ATOM   945  C  CG2 . THR A 1 139 ? -44.078 -3.123  1.396   1.00 32.74 ? 139 THR A CG2 1 
ATOM   946  N  N   . GLN A 1 140 ? -40.656 -2.711  2.148   1.00 24.11 ? 140 GLN A N   1 
ATOM   947  C  CA  . GLN A 1 140 ? -39.554 -3.605  1.853   1.00 25.14 ? 140 GLN A CA  1 
ATOM   948  C  C   . GLN A 1 140 ? -40.078 -5.041  1.793   1.00 27.69 ? 140 GLN A C   1 
ATOM   949  O  O   . GLN A 1 140 ? -40.976 -5.418  2.555   1.00 28.63 ? 140 GLN A O   1 
ATOM   950  C  CB  . GLN A 1 140 ? -38.442 -3.542  2.906   1.00 26.29 ? 140 GLN A CB  1 
ATOM   951  C  CG  . GLN A 1 140 ? -37.975 -2.099  3.081   1.00 27.06 ? 140 GLN A CG  1 
ATOM   952  C  CD  . GLN A 1 140 ? -36.763 -1.928  3.973   1.00 28.65 ? 140 GLN A CD  1 
ATOM   953  O  OE1 . GLN A 1 140 ? -36.579 -0.830  4.497   1.00 27.41 ? 140 GLN A OE1 1 
ATOM   954  N  NE2 . GLN A 1 140 ? -35.892 -2.927  4.093   1.00 28.38 ? 140 GLN A NE2 1 
ATOM   955  N  N   . SER A 1 141 ? -39.445 -5.851  0.953   1.00 26.36 ? 141 SER A N   1 
ATOM   956  C  CA  . SER A 1 141 ? -39.855 -7.242  0.818   1.00 27.25 ? 141 SER A CA  1 
ATOM   957  C  C   . SER A 1 141 ? -38.614 -8.044  0.487   1.00 27.44 ? 141 SER A C   1 
ATOM   958  O  O   . SER A 1 141 ? -37.896 -7.650  -0.448  1.00 30.46 ? 141 SER A O   1 
ATOM   959  C  CB  . SER A 1 141 ? -40.858 -7.312  -0.318  1.00 28.84 ? 141 SER A CB  1 
ATOM   960  O  OG  . SER A 1 141 ? -41.241 -8.683  -0.462  1.00 34.20 ? 141 SER A OG  1 
ATOM   961  N  N   . PRO A 1 142 ? -38.260 -9.157  1.173   1.00 26.45 ? 142 PRO A N   1 
ATOM   962  C  CA  . PRO A 1 142 ? -38.927 -9.637  2.384   1.00 29.08 ? 142 PRO A CA  1 
ATOM   963  C  C   . PRO A 1 142 ? -38.558 -8.761  3.591   1.00 30.64 ? 142 PRO A C   1 
ATOM   964  O  O   . PRO A 1 142 ? -37.697 -7.881  3.492   1.00 28.15 ? 142 PRO A O   1 
ATOM   965  C  CB  . PRO A 1 142 ? -38.277 -11.033 2.528   1.00 29.92 ? 142 PRO A CB  1 
ATOM   966  C  CG  . PRO A 1 142 ? -36.868 -10.825 2.035   1.00 30.00 ? 142 PRO A CG  1 
ATOM   967  C  CD  . PRO A 1 142 ? -37.078 -9.945  0.833   1.00 29.64 ? 142 PRO A CD  1 
ATOM   968  N  N   . THR A 1 143 ? -39.192 -9.005  4.735   1.00 30.17 ? 143 THR A N   1 
ATOM   969  C  CA  . THR A 1 143 ? -38.809 -8.233  5.920   1.00 29.79 ? 143 THR A CA  1 
ATOM   970  C  C   . THR A 1 143 ? -37.758 -8.979  6.741   1.00 28.34 ? 143 THR A C   1 
ATOM   971  O  O   . THR A 1 143 ? -37.150 -8.402  7.633   1.00 29.21 ? 143 THR A O   1 
ATOM   972  C  CB  . THR A 1 143 ? -40.014 -7.806  6.756   1.00 34.80 ? 143 THR A CB  1 
ATOM   973  O  OG1 . THR A 1 143 ? -40.618 -9.045  7.051   1.00 42.02 ? 143 THR A OG1 1 
ATOM   974  C  CG2 . THR A 1 143 ? -41.122 -7.134  5.974   1.00 34.05 ? 143 THR A CG2 1 
ATOM   975  N  N   . SER A 1 144 ? -37.557 -10.280 6.465   1.00 29.53 ? 144 SER A N   1 
ATOM   976  C  CA  . SER A 1 144 ? -36.408 -10.971 7.019   1.00 30.33 ? 144 SER A CA  1 
ATOM   977  C  C   . SER A 1 144 ? -36.011 -12.104 6.088   1.00 31.50 ? 144 SER A C   1 
ATOM   978  O  O   . SER A 1 144 ? -36.882 -12.653 5.419   1.00 31.38 ? 144 SER A O   1 
ATOM   979  C  CB  . SER A 1 144 ? -36.656 -11.455 8.430   1.00 37.20 ? 144 SER A CB  1 
ATOM   980  O  OG  . SER A 1 144 ? -37.658 -12.454 8.430   1.00 40.83 ? 144 SER A OG  1 
ATOM   981  N  N   . LEU A 1 145 ? -34.730 -12.487 6.137   1.00 29.79 ? 145 LEU A N   1 
ATOM   982  C  CA  . LEU A 1 145 ? -34.274 -13.558 5.270   1.00 31.34 ? 145 LEU A CA  1 
ATOM   983  C  C   . LEU A 1 145 ? -32.972 -14.101 5.831   1.00 31.59 ? 145 LEU A C   1 
ATOM   984  O  O   . LEU A 1 145 ? -32.269 -13.388 6.539   1.00 30.39 ? 145 LEU A O   1 
ATOM   985  C  CB  . LEU A 1 145 ? -34.175 -13.299 3.759   1.00 33.75 ? 145 LEU A CB  1 
ATOM   986  C  CG  . LEU A 1 145 ? -32.989 -12.433 3.325   1.00 32.01 ? 145 LEU A CG  1 
ATOM   987  C  CD1 . LEU A 1 145 ? -32.947 -12.415 1.798   1.00 38.02 ? 145 LEU A CD1 1 
ATOM   988  C  CD2 . LEU A 1 145 ? -33.237 -11.006 3.848   1.00 33.73 ? 145 LEU A CD2 1 
ATOM   989  N  N   . ALA A 1 146 ? -32.760 -15.410 5.599   1.00 30.88 ? 146 ALA A N   1 
ATOM   990  C  CA  . ALA A 1 146 ? -31.529 -16.062 6.002   1.00 31.15 ? 146 ALA A CA  1 
ATOM   991  C  C   . ALA A 1 146 ? -30.914 -16.595 4.726   1.00 32.35 ? 146 ALA A C   1 
ATOM   992  O  O   . ALA A 1 146 ? -31.576 -17.345 4.013   1.00 31.78 ? 146 ALA A O   1 
ATOM   993  C  CB  . ALA A 1 146 ? -31.835 -17.206 7.014   1.00 32.63 ? 146 ALA A CB  1 
ATOM   994  N  N   . VAL A 1 147 ? -29.636 -16.308 4.498   1.00 33.29 ? 147 VAL A N   1 
ATOM   995  C  CA  . VAL A 1 147 ? -28.990 -16.688 3.250   1.00 34.33 ? 147 VAL A CA  1 
ATOM   996  C  C   . VAL A 1 147 ? -27.675 -17.396 3.597   1.00 33.92 ? 147 VAL A C   1 
ATOM   997  O  O   . VAL A 1 147 ? -26.980 -16.971 4.532   1.00 35.46 ? 147 VAL A O   1 
ATOM   998  C  CB  . VAL A 1 147 ? -28.769 -15.331 2.508   1.00 36.73 ? 147 VAL A CB  1 
ATOM   999  C  CG1 . VAL A 1 147 ? -27.758 -15.499 1.384   1.00 35.15 ? 147 VAL A CG1 1 
ATOM   1000 C  CG2 . VAL A 1 147 ? -30.073 -14.773 1.904   1.00 34.71 ? 147 VAL A CG2 1 
ATOM   1001 N  N   . SER A 1 148 ? -27.300 -18.480 2.874   1.00 34.53 ? 148 SER A N   1 
ATOM   1002 C  CA  . SER A 1 148 ? -26.060 -19.131 3.296   1.00 34.18 ? 148 SER A CA  1 
ATOM   1003 C  C   . SER A 1 148 ? -24.850 -18.374 2.767   1.00 35.12 ? 148 SER A C   1 
ATOM   1004 O  O   . SER A 1 148 ? -24.931 -17.589 1.819   1.00 36.56 ? 148 SER A O   1 
ATOM   1005 C  CB  . SER A 1 148 ? -25.963 -20.589 2.890   1.00 42.41 ? 148 SER A CB  1 
ATOM   1006 O  OG  . SER A 1 148 ? -27.232 -21.217 2.969   1.00 48.69 ? 148 SER A OG  1 
ATOM   1007 N  N   . LEU A 1 149 ? -23.724 -18.598 3.431   1.00 34.13 ? 149 LEU A N   1 
ATOM   1008 C  CA  . LEU A 1 149 ? -22.494 -17.938 3.055   1.00 36.55 ? 149 LEU A CA  1 
ATOM   1009 C  C   . LEU A 1 149 ? -22.244 -18.180 1.576   1.00 38.68 ? 149 LEU A C   1 
ATOM   1010 O  O   . LEU A 1 149 ? -22.432 -19.300 1.073   1.00 37.85 ? 149 LEU A O   1 
ATOM   1011 C  CB  . LEU A 1 149 ? -21.336 -18.497 3.869   1.00 37.06 ? 149 LEU A CB  1 
ATOM   1012 C  CG  . LEU A 1 149 ? -21.168 -17.964 5.286   1.00 45.45 ? 149 LEU A CG  1 
ATOM   1013 C  CD1 . LEU A 1 149 ? -19.928 -18.666 5.833   1.00 48.77 ? 149 LEU A CD1 1 
ATOM   1014 C  CD2 . LEU A 1 149 ? -20.976 -16.449 5.369   1.00 47.18 ? 149 LEU A CD2 1 
ATOM   1015 N  N   . GLY A 1 150 ? -21.819 -17.127 0.874   1.00 36.04 ? 150 GLY A N   1 
ATOM   1016 C  CA  . GLY A 1 150 ? -21.509 -17.310 -0.540  1.00 37.03 ? 150 GLY A CA  1 
ATOM   1017 C  C   . GLY A 1 150 ? -22.703 -17.119 -1.472  1.00 35.35 ? 150 GLY A C   1 
ATOM   1018 O  O   . GLY A 1 150 ? -22.508 -16.953 -2.674  1.00 39.99 ? 150 GLY A O   1 
ATOM   1019 N  N   . GLN A 1 151 ? -23.934 -17.111 -0.958  1.00 32.85 ? 151 GLN A N   1 
ATOM   1020 C  CA  . GLN A 1 151 ? -25.104 -16.995 -1.816  1.00 32.93 ? 151 GLN A CA  1 
ATOM   1021 C  C   . GLN A 1 151 ? -25.541 -15.531 -1.941  1.00 34.94 ? 151 GLN A C   1 
ATOM   1022 O  O   . GLN A 1 151 ? -24.836 -14.648 -1.474  1.00 33.20 ? 151 GLN A O   1 
ATOM   1023 C  CB  . GLN A 1 151 ? -26.183 -17.900 -1.227  1.00 36.08 ? 151 GLN A CB  1 
ATOM   1024 C  CG  . GLN A 1 151 ? -25.814 -19.384 -1.240  1.00 40.37 ? 151 GLN A CG  1 
ATOM   1025 C  CD  . GLN A 1 151 ? -25.723 -19.926 -2.650  0.80 46.68 ? 151 GLN A CD  1 
ATOM   1026 O  OE1 . GLN A 1 151 ? -24.629 -20.056 -3.215  0.80 48.17 ? 151 GLN A OE1 1 
ATOM   1027 N  NE2 . GLN A 1 151 ? -26.882 -20.178 -3.249  0.80 46.66 ? 151 GLN A NE2 1 
ATOM   1028 N  N   . ARG A 1 152 ? -26.674 -15.271 -2.613  1.00 32.51 ? 152 ARG A N   1 
ATOM   1029 C  CA  . ARG A 1 152 ? -27.163 -13.916 -2.916  1.00 29.14 ? 152 ARG A CA  1 
ATOM   1030 C  C   . ARG A 1 152 ? -28.354 -13.550 -2.027  1.00 28.79 ? 152 ARG A C   1 
ATOM   1031 O  O   . ARG A 1 152 ? -29.285 -14.355 -1.791  1.00 29.59 ? 152 ARG A O   1 
ATOM   1032 C  CB  . ARG A 1 152 ? -27.628 -13.850 -4.383  1.00 31.75 ? 152 ARG A CB  1 
ATOM   1033 C  CG  . ARG A 1 152 ? -28.272 -12.559 -4.852  1.00 32.80 ? 152 ARG A CG  1 
ATOM   1034 C  CD  . ARG A 1 152 ? -28.429 -12.595 -6.381  1.00 33.73 ? 152 ARG A CD  1 
ATOM   1035 N  NE  . ARG A 1 152 ? -27.135 -12.617 -7.076  1.00 31.63 ? 152 ARG A NE  1 
ATOM   1036 C  CZ  . ARG A 1 152 ? -26.366 -11.561 -7.321  1.00 35.57 ? 152 ARG A CZ  1 
ATOM   1037 N  NH1 . ARG A 1 152 ? -26.732 -10.346 -6.940  1.00 30.84 ? 152 ARG A NH1 1 
ATOM   1038 N  NH2 . ARG A 1 152 ? -25.232 -11.719 -7.987  1.00 36.82 ? 152 ARG A NH2 1 
ATOM   1039 N  N   . ALA A 1 153 ? -28.328 -12.319 -1.510  1.00 25.94 ? 153 ALA A N   1 
ATOM   1040 C  CA  . ALA A 1 153 ? -29.500 -11.727 -0.915  1.00 27.31 ? 153 ALA A CA  1 
ATOM   1041 C  C   . ALA A 1 153 ? -30.015 -10.603 -1.825  1.00 30.03 ? 153 ALA A C   1 
ATOM   1042 O  O   . ALA A 1 153 ? -29.240 -9.758  -2.300  1.00 29.38 ? 153 ALA A O   1 
ATOM   1043 C  CB  . ALA A 1 153 ? -29.105 -11.146 0.429   1.00 27.85 ? 153 ALA A CB  1 
ATOM   1044 N  N   . THR A 1 154 ? -31.337 -10.558 -2.009  1.00 27.15 ? 154 THR A N   1 
ATOM   1045 C  CA  . THR A 1 154 ? -31.961 -9.550  -2.861  1.00 28.06 ? 154 THR A CA  1 
ATOM   1046 C  C   . THR A 1 154 ? -33.176 -9.011  -2.114  1.00 26.52 ? 154 THR A C   1 
ATOM   1047 O  O   . THR A 1 154 ? -33.999 -9.796  -1.598  1.00 30.33 ? 154 THR A O   1 
ATOM   1048 C  CB  . THR A 1 154 ? -32.409 -10.233 -4.157  1.00 28.80 ? 154 THR A CB  1 
ATOM   1049 O  OG1 . THR A 1 154 ? -31.313 -10.850 -4.838  1.00 30.67 ? 154 THR A OG1 1 
ATOM   1050 C  CG2 . THR A 1 154 ? -33.186 -9.291  -5.054  1.00 27.78 ? 154 THR A CG2 1 
ATOM   1051 N  N   . ILE A 1 155 ? -33.246 -7.683  -1.995  1.00 24.65 ? 155 ILE A N   1 
ATOM   1052 C  CA  . ILE A 1 155 ? -34.247 -7.038  -1.164  1.00 27.89 ? 155 ILE A CA  1 
ATOM   1053 C  C   . ILE A 1 155 ? -34.866 -5.944  -2.005  1.00 28.87 ? 155 ILE A C   1 
ATOM   1054 O  O   . ILE A 1 155 ? -34.140 -5.143  -2.610  1.00 30.16 ? 155 ILE A O   1 
ATOM   1055 C  CB  . ILE A 1 155 ? -33.597 -6.463  0.127   1.00 27.87 ? 155 ILE A CB  1 
ATOM   1056 C  CG1 . ILE A 1 155 ? -32.874 -7.547  0.963   1.00 27.94 ? 155 ILE A CG1 1 
ATOM   1057 C  CG2 . ILE A 1 155 ? -34.619 -5.713  0.985   1.00 28.29 ? 155 ILE A CG2 1 
ATOM   1058 C  CD1 . ILE A 1 155 ? -32.097 -6.963  2.162   1.00 28.16 ? 155 ILE A CD1 1 
ATOM   1059 N  N   . SER A 1 156 ? -36.186 -5.900  -1.994  1.00 25.28 ? 156 SER A N   1 
ATOM   1060 C  CA  . SER A 1 156 ? -36.953 -4.926  -2.736  1.00 27.10 ? 156 SER A CA  1 
ATOM   1061 C  C   . SER A 1 156 ? -37.429 -3.812  -1.800  1.00 27.60 ? 156 SER A C   1 
ATOM   1062 O  O   . SER A 1 156 ? -37.817 -4.042  -0.653  1.00 28.72 ? 156 SER A O   1 
ATOM   1063 C  CB  . SER A 1 156 ? -38.116 -5.645  -3.361  1.00 29.69 ? 156 SER A CB  1 
ATOM   1064 O  OG  . SER A 1 156 ? -39.081 -4.755  -3.877  1.00 30.42 ? 156 SER A OG  1 
ATOM   1065 N  N   . CYS A 1 157 ? -37.433 -2.578  -2.334  1.00 27.86 ? 157 CYS A N   1 
ATOM   1066 C  CA  . CYS A 1 157 ? -38.082 -1.449  -1.686  1.00 27.55 ? 157 CYS A CA  1 
ATOM   1067 C  C   . CYS A 1 157 ? -38.950 -0.770  -2.754  1.00 30.76 ? 157 CYS A C   1 
ATOM   1068 O  O   . CYS A 1 157 ? -38.446 -0.328  -3.799  1.00 31.38 ? 157 CYS A O   1 
ATOM   1069 C  CB  . CYS A 1 157 ? -37.013 -0.463  -1.224  1.00 31.15 ? 157 CYS A CB  1 
ATOM   1070 S  SG  . CYS A 1 157 ? -37.726 1.090   -0.632  1.00 35.82 ? 157 CYS A SG  1 
ATOM   1071 N  N   . LYS A 1 158 ? -40.233 -0.627  -2.448  1.00 28.35 ? 158 LYS A N   1 
ATOM   1072 C  CA  . LYS A 1 158 ? -41.134 0.022   -3.400  1.00 29.24 ? 158 LYS A CA  1 
ATOM   1073 C  C   . LYS A 1 158 ? -41.806 1.203   -2.719  1.00 30.98 ? 158 LYS A C   1 
ATOM   1074 O  O   . LYS A 1 158 ? -42.248 1.037   -1.572  1.00 31.30 ? 158 LYS A O   1 
ATOM   1075 C  CB  . LYS A 1 158 ? -42.241 -0.965  -3.822  1.00 30.60 ? 158 LYS A CB  1 
ATOM   1076 C  CG  . LYS A 1 158 ? -41.658 -2.053  -4.716  1.00 31.93 ? 158 LYS A CG  1 
ATOM   1077 C  CD  . LYS A 1 158 ? -42.719 -3.047  -5.199  1.00 34.90 ? 158 LYS A CD  1 
ATOM   1078 C  CE  . LYS A 1 158 ? -42.130 -4.173  -6.028  1.00 39.97 ? 158 LYS A CE  1 
ATOM   1079 N  NZ  . LYS A 1 158 ? -43.180 -5.093  -6.531  1.00 40.43 ? 158 LYS A NZ  1 
ATOM   1080 N  N   . ALA A 1 159 ? -41.859 2.361   -3.433  1.00 28.44 ? 159 ALA A N   1 
ATOM   1081 C  CA  . ALA A 1 159 ? -42.394 3.601   -2.880  1.00 27.73 ? 159 ALA A CA  1 
ATOM   1082 C  C   . ALA A 1 159 ? -43.825 3.797   -3.390  1.00 32.08 ? 159 ALA A C   1 
ATOM   1083 O  O   . ALA A 1 159 ? -44.106 3.473   -4.535  1.00 31.68 ? 159 ALA A O   1 
ATOM   1084 C  CB  . ALA A 1 159 ? -41.544 4.802   -3.308  1.00 26.35 ? 159 ALA A CB  1 
ATOM   1085 N  N   . SER A 1 160 ? -44.673 4.456   -2.605  1.00 32.10 ? 160 SER A N   1 
ATOM   1086 C  CA  . SER A 1 160 ? -46.044 4.708   -3.020  1.00 32.44 ? 160 SER A CA  1 
ATOM   1087 C  C   . SER A 1 160 ? -46.133 5.770   -4.127  1.00 35.28 ? 160 SER A C   1 
ATOM   1088 O  O   . SER A 1 160 ? -47.136 5.866   -4.807  1.00 36.73 ? 160 SER A O   1 
ATOM   1089 C  CB  . SER A 1 160 ? -46.891 5.073   -1.843  1.00 35.51 ? 160 SER A CB  1 
ATOM   1090 O  OG  . SER A 1 160 ? -46.420 6.234   -1.177  1.00 33.18 ? 160 SER A OG  1 
ATOM   1091 N  N   . GLN A 1 161 ? -45.147 6.661   -4.234  1.00 31.96 ? 161 GLN A N   1 
ATOM   1092 C  CA  . GLN A 1 161 ? -45.060 7.627   -5.317  1.00 36.38 ? 161 GLN A CA  1 
ATOM   1093 C  C   . GLN A 1 161 ? -43.596 7.710   -5.727  1.00 36.09 ? 161 GLN A C   1 
ATOM   1094 O  O   . GLN A 1 161 ? -42.705 7.284   -4.975  1.00 33.08 ? 161 GLN A O   1 
ATOM   1095 C  CB  . GLN A 1 161 ? -45.412 9.048   -4.879  1.00 38.43 ? 161 GLN A CB  1 
ATOM   1096 C  CG  . GLN A 1 161 ? -46.801 9.213   -4.276  1.00 46.96 ? 161 GLN A CG  1 
ATOM   1097 C  CD  . GLN A 1 161 ? -46.949 10.526  -3.531  0.70 53.82 ? 161 GLN A CD  1 
ATOM   1098 O  OE1 . GLN A 1 161 ? -47.383 10.565  -2.373  0.70 52.22 ? 161 GLN A OE1 1 
ATOM   1099 N  NE2 . GLN A 1 161 ? -46.579 11.627  -4.179  0.70 59.66 ? 161 GLN A NE2 1 
ATOM   1100 N  N   . SER A 1 162 ? -43.364 8.283   -6.912  1.00 33.82 ? 162 SER A N   1 
ATOM   1101 C  CA  . SER A 1 162 ? -42.027 8.426   -7.464  1.00 36.66 ? 162 SER A CA  1 
ATOM   1102 C  C   . SER A 1 162 ? -41.108 9.217   -6.531  1.00 35.67 ? 162 SER A C   1 
ATOM   1103 O  O   . SER A 1 162 ? -41.510 10.233  -5.963  1.00 34.58 ? 162 SER A O   1 
ATOM   1104 C  CB  . SER A 1 162 ? -42.098 9.123   -8.802  1.00 36.61 ? 162 SER A CB  1 
ATOM   1105 O  OG  . SER A 1 162 ? -40.769 9.325   -9.281  1.00 35.58 ? 162 SER A OG  1 
ATOM   1106 N  N   . VAL A 1 163 ? -39.853 8.769   -6.418  1.00 31.79 ? 163 VAL A N   1 
ATOM   1107 C  CA  . VAL A 1 163 ? -38.894 9.505   -5.613  1.00 32.10 ? 163 VAL A CA  1 
ATOM   1108 C  C   . VAL A 1 163 ? -37.827 10.089  -6.534  1.00 34.69 ? 163 VAL A C   1 
ATOM   1109 O  O   . VAL A 1 163 ? -36.755 10.459  -6.054  1.00 35.90 ? 163 VAL A O   1 
ATOM   1110 C  CB  . VAL A 1 163 ? -38.289 8.619   -4.505  1.00 32.97 ? 163 VAL A CB  1 
ATOM   1111 C  CG1 . VAL A 1 163 ? -39.404 8.120   -3.575  1.00 33.24 ? 163 VAL A CG1 1 
ATOM   1112 C  CG2 . VAL A 1 163 ? -37.499 7.435   -5.089  1.00 33.18 ? 163 VAL A CG2 1 
ATOM   1113 N  N   . ASP A 1 164 ? -38.146 10.216  -7.829  1.00 34.17 ? 164 ASP A N   1 
ATOM   1114 C  CA  . ASP A 1 164 ? -37.140 10.739  -8.748  1.00 33.54 ? 164 ASP A CA  1 
ATOM   1115 C  C   . ASP A 1 164 ? -37.291 12.245  -8.961  1.00 34.34 ? 164 ASP A C   1 
ATOM   1116 O  O   . ASP A 1 164 ? -38.387 12.788  -8.901  1.00 34.63 ? 164 ASP A O   1 
ATOM   1117 C  CB  . ASP A 1 164 ? -37.133 9.994   -10.064 1.00 37.82 ? 164 ASP A CB  1 
ATOM   1118 C  CG  . ASP A 1 164 ? -36.595 8.571   -9.996  1.00 39.82 ? 164 ASP A CG  1 
ATOM   1119 O  OD1 . ASP A 1 164 ? -36.148 8.126   -8.898  1.00 40.39 ? 164 ASP A OD1 1 
ATOM   1120 O  OD2 . ASP A 1 164 ? -36.549 7.953   -11.045 1.00 41.73 ? 164 ASP A OD2 1 
ATOM   1121 N  N   . TYR A 1 165 ? -36.155 12.912  -9.228  1.00 32.19 ? 165 TYR A N   1 
ATOM   1122 C  CA  . TYR A 1 165 ? -36.167 14.286  -9.703  1.00 34.41 ? 165 TYR A CA  1 
ATOM   1123 C  C   . TYR A 1 165 ? -34.984 14.472  -10.644 1.00 37.40 ? 165 TYR A C   1 
ATOM   1124 O  O   . TYR A 1 165 ? -33.855 14.095  -10.310 1.00 32.87 ? 165 TYR A O   1 
ATOM   1125 C  CB  . TYR A 1 165 ? -36.049 15.220  -8.504  1.00 34.00 ? 165 TYR A CB  1 
ATOM   1126 C  CG  . TYR A 1 165 ? -35.871 16.651  -8.976  1.00 39.93 ? 165 TYR A CG  1 
ATOM   1127 C  CD1 . TYR A 1 165 ? -36.971 17.390  -9.401  1.00 38.63 ? 165 TYR A CD1 1 
ATOM   1128 C  CD2 . TYR A 1 165 ? -34.608 17.243  -9.007  1.00 37.82 ? 165 TYR A CD2 1 
ATOM   1129 C  CE1 . TYR A 1 165 ? -36.818 18.688  -9.866  1.00 38.15 ? 165 TYR A CE1 1 
ATOM   1130 C  CE2 . TYR A 1 165 ? -34.442 18.533  -9.501  1.00 41.00 ? 165 TYR A CE2 1 
ATOM   1131 C  CZ  . TYR A 1 165 ? -35.554 19.255  -9.903  1.00 41.74 ? 165 TYR A CZ  1 
ATOM   1132 O  OH  . TYR A 1 165 ? -35.384 20.529  -10.347 1.00 42.31 ? 165 TYR A OH  1 
ATOM   1133 N  N   . ASP A 1 166 ? -35.262 15.044  -11.827 1.00 37.12 ? 166 ASP A N   1 
ATOM   1134 C  CA  . ASP A 1 166 ? -34.233 15.354  -12.805 1.00 38.76 ? 166 ASP A CA  1 
ATOM   1135 C  C   . ASP A 1 166 ? -33.361 14.133  -13.109 1.00 39.42 ? 166 ASP A C   1 
ATOM   1136 O  O   . ASP A 1 166 ? -32.143 14.263  -13.237 1.00 44.86 ? 166 ASP A O   1 
ATOM   1137 C  CB  . ASP A 1 166 ? -33.432 16.565  -12.347 1.00 41.66 ? 166 ASP A CB  1 
ATOM   1138 C  CG  . ASP A 1 166 ? -32.406 17.090  -13.344 1.00 53.69 ? 166 ASP A CG  1 
ATOM   1139 O  OD1 . ASP A 1 166 ? -32.762 17.135  -14.545 1.00 46.79 ? 166 ASP A OD1 1 
ATOM   1140 O  OD2 . ASP A 1 166 ? -31.260 17.427  -12.909 1.00 49.12 ? 166 ASP A OD2 1 
ATOM   1141 N  N   . GLY A 1 167 ? -33.965 12.943  -13.219 1.00 35.78 ? 167 GLY A N   1 
ATOM   1142 C  CA  . GLY A 1 167 ? -33.166 11.773  -13.578 1.00 42.46 ? 167 GLY A CA  1 
ATOM   1143 C  C   . GLY A 1 167 ? -32.370 11.136  -12.421 1.00 44.11 ? 167 GLY A C   1 
ATOM   1144 O  O   . GLY A 1 167 ? -31.683 10.130  -12.628 1.00 46.29 ? 167 GLY A O   1 
ATOM   1145 N  N   . ASP A 1 168 ? -32.429 11.716  -11.214 1.00 38.34 ? 168 ASP A N   1 
ATOM   1146 C  CA  . ASP A 1 168 ? -31.771 11.150  -10.023 1.00 36.03 ? 168 ASP A CA  1 
ATOM   1147 C  C   . ASP A 1 168 ? -32.822 10.615  -9.051  1.00 34.21 ? 168 ASP A C   1 
ATOM   1148 O  O   . ASP A 1 168 ? -33.855 11.254  -8.861  1.00 34.04 ? 168 ASP A O   1 
ATOM   1149 C  CB  . ASP A 1 168 ? -31.075 12.243  -9.224  1.00 36.06 ? 168 ASP A CB  1 
ATOM   1150 C  CG  . ASP A 1 168 ? -29.945 12.951  -9.946  1.00 42.17 ? 168 ASP A CG  1 
ATOM   1151 O  OD1 . ASP A 1 168 ? -29.227 12.260  -10.702 1.00 42.86 ? 168 ASP A OD1 1 
ATOM   1152 O  OD2 . ASP A 1 168 ? -29.785 14.167  -9.727  1.00 45.69 ? 168 ASP A OD2 1 
ATOM   1153 N  N   . SER A 1 169 ? -32.559 9.443   -8.445  1.00 32.20 ? 169 SER A N   1 
ATOM   1154 C  CA  . SER A 1 169 ? -33.474 8.883   -7.465  1.00 30.04 ? 169 SER A CA  1 
ATOM   1155 C  C   . SER A 1 169 ? -33.035 9.296   -6.071  1.00 27.86 ? 169 SER A C   1 
ATOM   1156 O  O   . SER A 1 169 ? -31.895 9.022   -5.713  1.00 35.09 ? 169 SER A O   1 
ATOM   1157 C  CB  . SER A 1 169 ? -33.415 7.380   -7.511  1.00 29.08 ? 169 SER A CB  1 
ATOM   1158 O  OG  . SER A 1 169 ? -33.951 6.913   -8.718  1.00 31.75 ? 169 SER A OG  1 
ATOM   1159 N  N   . TYR A 1 170 ? -33.900 10.044  -5.369  1.00 28.77 ? 170 TYR A N   1 
ATOM   1160 C  CA  . TYR A 1 170 ? -33.712 10.499  -4.001  1.00 29.79 ? 170 TYR A CA  1 
ATOM   1161 C  C   . TYR A 1 170 ? -34.050 9.356   -3.044  1.00 31.64 ? 170 TYR A C   1 
ATOM   1162 O  O   . TYR A 1 170 ? -34.914 9.497   -2.195  1.00 27.78 ? 170 TYR A O   1 
ATOM   1163 C  CB  . TYR A 1 170 ? -34.478 11.793  -3.670  1.00 28.15 ? 170 TYR A CB  1 
ATOM   1164 C  CG  . TYR A 1 170 ? -33.744 12.961  -4.337  1.00 30.64 ? 170 TYR A CG  1 
ATOM   1165 C  CD1 . TYR A 1 170 ? -33.687 13.088  -5.743  1.00 31.68 ? 170 TYR A CD1 1 
ATOM   1166 C  CD2 . TYR A 1 170 ? -33.071 13.903  -3.548  1.00 32.31 ? 170 TYR A CD2 1 
ATOM   1167 C  CE1 . TYR A 1 170 ? -32.967 14.121  -6.348  1.00 32.57 ? 170 TYR A CE1 1 
ATOM   1168 C  CE2 . TYR A 1 170 ? -32.369 14.949  -4.155  1.00 33.53 ? 170 TYR A CE2 1 
ATOM   1169 C  CZ  . TYR A 1 170 ? -32.309 15.045  -5.543  1.00 36.39 ? 170 TYR A CZ  1 
ATOM   1170 O  OH  . TYR A 1 170 ? -31.597 16.096  -6.097  1.00 36.93 ? 170 TYR A OH  1 
ATOM   1171 N  N   . MET A 1 171 ? -33.349 8.257   -3.243  1.00 28.42 ? 171 MET A N   1 
ATOM   1172 C  CA  A MET A 1 171 ? -33.470 7.105   -2.312  0.50 26.07 ? 171 MET A CA  1 
ATOM   1173 C  CA  B MET A 1 171 ? -33.471 7.067   -2.349  0.50 29.77 ? 171 MET A CA  1 
ATOM   1174 C  C   . MET A 1 171 ? -32.065 6.493   -1.922  1.00 27.86 ? 171 MET A C   1 
ATOM   1175 O  O   . MET A 1 171 ? -30.988 6.396   -2.669  1.00 27.42 ? 171 MET A O   1 
ATOM   1176 C  CB  A MET A 1 171 ? -34.356 6.008   -2.917  0.50 23.45 ? 171 MET A CB  1 
ATOM   1177 C  CB  B MET A 1 171 ? -34.264 5.949   -3.045  0.50 32.17 ? 171 MET A CB  1 
ATOM   1178 C  CG  A MET A 1 171 ? -33.646 5.098   -3.883  0.50 21.76 ? 171 MET A CG  1 
ATOM   1179 C  CG  B MET A 1 171 ? -33.551 4.610   -3.140  0.50 36.12 ? 171 MET A CG  1 
ATOM   1180 S  SD  A MET A 1 171 ? -32.975 3.648   -3.048  0.50 24.62 ? 171 MET A SD  1 
ATOM   1181 S  SD  B MET A 1 171 ? -34.164 3.456   -1.898  0.50 42.76 ? 171 MET A SD  1 
ATOM   1182 C  CE  A MET A 1 171 ? -34.263 3.375   -1.824  0.50 27.41 ? 171 MET A CE  1 
ATOM   1183 C  CE  B MET A 1 171 ? -35.753 4.218   -1.547  0.50 33.97 ? 171 MET A CE  1 
ATOM   1184 N  N   . ASN A 1 172 ? -31.972 6.227   -0.617  1.00 24.73 ? 172 ASN A N   1 
ATOM   1185 C  CA  . ASN A 1 172 ? -30.731 5.655   -0.103  1.00 24.39 ? 172 ASN A CA  1 
ATOM   1186 C  C   . ASN A 1 172 ? -31.064 4.344   0.613   1.00 25.26 ? 172 ASN A C   1 
ATOM   1187 O  O   . ASN A 1 172 ? -32.205 4.160   1.039   1.00 26.25 ? 172 ASN A O   1 
ATOM   1188 C  CB  . ASN A 1 172 ? -30.080 6.571   0.943   1.00 23.07 ? 172 ASN A CB  1 
ATOM   1189 C  CG  . ASN A 1 172 ? -29.831 7.981   0.421   1.00 28.32 ? 172 ASN A CG  1 
ATOM   1190 O  OD1 . ASN A 1 172 ? -29.612 8.187   -0.775  1.00 25.26 ? 172 ASN A OD1 1 
ATOM   1191 N  ND2 . ASN A 1 172 ? -29.808 8.968   1.310   1.00 25.21 ? 172 ASN A ND2 1 
ATOM   1192 N  N   . TRP A 1 173 ? -30.051 3.488   0.782   1.00 24.88 ? 173 TRP A N   1 
ATOM   1193 C  CA  . TRP A 1 173 ? -30.103 2.322   1.653   1.00 25.14 ? 173 TRP A CA  1 
ATOM   1194 C  C   . TRP A 1 173 ? -29.130 2.521   2.820   1.00 27.43 ? 173 TRP A C   1 
ATOM   1195 O  O   . TRP A 1 173 ? -28.021 3.051   2.650   1.00 26.83 ? 173 TRP A O   1 
ATOM   1196 C  CB  . TRP A 1 173 ? -29.680 1.078   0.868   1.00 27.07 ? 173 TRP A CB  1 
ATOM   1197 C  CG  . TRP A 1 173 ? -30.650 0.637   -0.195  1.00 24.10 ? 173 TRP A CG  1 
ATOM   1198 C  CD1 . TRP A 1 173 ? -30.617 0.906   -1.546  1.00 26.53 ? 173 TRP A CD1 1 
ATOM   1199 C  CD2 . TRP A 1 173 ? -31.762 -0.255  0.010   1.00 24.59 ? 173 TRP A CD2 1 
ATOM   1200 N  NE1 . TRP A 1 173 ? -31.659 0.271   -2.181  1.00 26.90 ? 173 TRP A NE1 1 
ATOM   1201 C  CE2 . TRP A 1 173 ? -32.379 -0.443  -1.256  1.00 26.70 ? 173 TRP A CE2 1 
ATOM   1202 C  CE3 . TRP A 1 173 ? -32.303 -0.884  1.140   1.00 24.18 ? 173 TRP A CE3 1 
ATOM   1203 C  CZ2 . TRP A 1 173 ? -33.491 -1.277  -1.442  1.00 29.35 ? 173 TRP A CZ2 1 
ATOM   1204 C  CZ3 . TRP A 1 173 ? -33.393 -1.727  0.952   1.00 26.03 ? 173 TRP A CZ3 1 
ATOM   1205 C  CH2 . TRP A 1 173 ? -33.982 -1.882  -0.310  1.00 27.85 ? 173 TRP A CH2 1 
ATOM   1206 N  N   . TYR A 1 174 ? -29.585 2.095   3.992   1.00 25.72 ? 174 TYR A N   1 
ATOM   1207 C  CA  . TYR A 1 174 ? -28.799 2.139   5.218   1.00 24.79 ? 174 TYR A CA  1 
ATOM   1208 C  C   . TYR A 1 174 ? -28.599 0.688   5.696   1.00 24.45 ? 174 TYR A C   1 
ATOM   1209 O  O   . TYR A 1 174 ? -29.479 -0.177  5.487   1.00 24.96 ? 174 TYR A O   1 
ATOM   1210 C  CB  . TYR A 1 174 ? -29.515 2.981   6.284   1.00 24.12 ? 174 TYR A CB  1 
ATOM   1211 C  CG  . TYR A 1 174 ? -29.520 4.434   5.849   1.00 24.99 ? 174 TYR A CG  1 
ATOM   1212 C  CD1 . TYR A 1 174 ? -28.434 5.277   6.131   1.00 25.31 ? 174 TYR A CD1 1 
ATOM   1213 C  CD2 . TYR A 1 174 ? -30.599 4.955   5.125   1.00 25.08 ? 174 TYR A CD2 1 
ATOM   1214 C  CE1 . TYR A 1 174 ? -28.401 6.608   5.671   1.00 27.08 ? 174 TYR A CE1 1 
ATOM   1215 C  CE2 . TYR A 1 174 ? -30.587 6.287   4.714   1.00 28.08 ? 174 TYR A CE2 1 
ATOM   1216 C  CZ  . TYR A 1 174 ? -29.487 7.091   4.944   1.00 27.64 ? 174 TYR A CZ  1 
ATOM   1217 O  OH  . TYR A 1 174 ? -29.515 8.344   4.364   1.00 26.14 ? 174 TYR A OH  1 
ATOM   1218 N  N   . GLN A 1 175 ? -27.449 0.442   6.343   1.00 25.87 ? 175 GLN A N   1 
ATOM   1219 C  CA  . GLN A 1 175 ? -27.199 -0.849  6.977   1.00 27.21 ? 175 GLN A CA  1 
ATOM   1220 C  C   . GLN A 1 175 ? -26.968 -0.601  8.469   1.00 25.96 ? 175 GLN A C   1 
ATOM   1221 O  O   . GLN A 1 175 ? -26.226 0.336   8.864   1.00 26.80 ? 175 GLN A O   1 
ATOM   1222 C  CB  . GLN A 1 175 ? -25.908 -1.390  6.371   1.00 26.84 ? 175 GLN A CB  1 
ATOM   1223 C  CG  . GLN A 1 175 ? -25.419 -2.709  6.968   1.00 26.60 ? 175 GLN A CG  1 
ATOM   1224 C  CD  . GLN A 1 175 ? -24.027 -3.054  6.473   1.00 29.22 ? 175 GLN A CD  1 
ATOM   1225 O  OE1 . GLN A 1 175 ? -23.077 -2.250  6.600   1.00 29.54 ? 175 GLN A OE1 1 
ATOM   1226 N  NE2 . GLN A 1 175 ? -23.872 -4.253  5.903   1.00 27.63 ? 175 GLN A NE2 1 
ATOM   1227 N  N   . GLN A 1 176 ? -27.551 -1.448  9.301   1.00 24.76 ? 176 GLN A N   1 
ATOM   1228 C  CA  . GLN A 1 176 ? -27.231 -1.441  10.725  1.00 25.42 ? 176 GLN A CA  1 
ATOM   1229 C  C   . GLN A 1 176 ? -26.772 -2.834  11.158  1.00 24.70 ? 176 GLN A C   1 
ATOM   1230 O  O   . GLN A 1 176 ? -27.601 -3.733  11.260  1.00 26.64 ? 176 GLN A O   1 
ATOM   1231 C  CB  . GLN A 1 176 ? -28.398 -0.991  11.593  1.00 25.33 ? 176 GLN A CB  1 
ATOM   1232 C  CG  . GLN A 1 176 ? -27.998 -0.902  13.071  1.00 28.85 ? 176 GLN A CG  1 
ATOM   1233 C  CD  . GLN A 1 176 ? -29.008 -0.197  13.942  1.00 28.88 ? 176 GLN A CD  1 
ATOM   1234 O  OE1 . GLN A 1 176 ? -30.219 -0.281  13.671  1.00 29.03 ? 176 GLN A OE1 1 
ATOM   1235 N  NE2 . GLN A 1 176 ? -28.491 0.587   14.901  1.00 27.74 ? 176 GLN A NE2 1 
ATOM   1236 N  N   . LYS A 1 177 ? -25.451 -2.997  11.303  1.00 27.48 ? 177 LYS A N   1 
ATOM   1237 C  CA  . LYS A 1 177 ? -24.941 -4.279  11.780  1.00 28.00 ? 177 LYS A CA  1 
ATOM   1238 C  C   . LYS A 1 177 ? -25.271 -4.394  13.271  1.00 31.08 ? 177 LYS A C   1 
ATOM   1239 O  O   . LYS A 1 177 ? -25.459 -3.394  13.974  1.00 29.09 ? 177 LYS A O   1 
ATOM   1240 C  CB  . LYS A 1 177 ? -23.419 -4.250  11.634  1.00 29.84 ? 177 LYS A CB  1 
ATOM   1241 C  CG  . LYS A 1 177 ? -23.027 -4.351  10.162  1.00 29.81 ? 177 LYS A CG  1 
ATOM   1242 C  CD  . LYS A 1 177 ? -21.506 -4.322  10.056  1.00 34.98 ? 177 LYS A CD  1 
ATOM   1243 C  CE  . LYS A 1 177 ? -21.096 -4.363  8.592   1.00 36.41 ? 177 LYS A CE  1 
ATOM   1244 N  NZ  . LYS A 1 177 ? -19.622 -4.293  8.550   1.00 40.31 ? 177 LYS A NZ  1 
ATOM   1245 N  N   . PRO A 1 178 ? -25.345 -5.628  13.822  1.00 30.81 ? 178 PRO A N   1 
ATOM   1246 C  CA  . PRO A 1 178 ? -25.704 -5.820  15.236  1.00 31.18 ? 178 PRO A CA  1 
ATOM   1247 C  C   . PRO A 1 178 ? -24.759 -5.082  16.184  1.00 32.50 ? 178 PRO A C   1 
ATOM   1248 O  O   . PRO A 1 178 ? -23.533 -5.131  16.027  1.00 31.55 ? 178 PRO A O   1 
ATOM   1249 C  CB  . PRO A 1 178 ? -25.658 -7.389  15.371  1.00 33.58 ? 178 PRO A CB  1 
ATOM   1250 C  CG  . PRO A 1 178 ? -25.942 -7.851  13.967  1.00 34.51 ? 178 PRO A CG  1 
ATOM   1251 C  CD  . PRO A 1 178 ? -25.095 -6.898  13.098  1.00 33.43 ? 178 PRO A CD  1 
ATOM   1252 N  N   . GLY A 1 179 ? -25.366 -4.247  17.043  1.00 32.09 ? 179 GLY A N   1 
ATOM   1253 C  CA  . GLY A 1 179 ? -24.654 -3.511  18.074  1.00 35.93 ? 179 GLY A CA  1 
ATOM   1254 C  C   . GLY A 1 179 ? -23.989 -2.235  17.553  1.00 34.93 ? 179 GLY A C   1 
ATOM   1255 O  O   . GLY A 1 179 ? -23.326 -1.553  18.327  1.00 34.51 ? 179 GLY A O   1 
ATOM   1256 N  N   . GLN A 1 180 ? -24.185 -1.911  16.256  1.00 32.34 ? 180 GLN A N   1 
ATOM   1257 C  CA  A GLN A 1 180 ? -23.483 -0.791  15.632  0.70 30.94 ? 180 GLN A CA  1 
ATOM   1258 C  CA  B GLN A 1 180 ? -23.484 -0.798  15.632  0.30 31.21 ? 180 GLN A CA  1 
ATOM   1259 C  C   . GLN A 1 180 ? -24.499 0.288   15.253  1.00 31.49 ? 180 GLN A C   1 
ATOM   1260 O  O   . GLN A 1 180 ? -25.696 0.022   15.110  1.00 28.29 ? 180 GLN A O   1 
ATOM   1261 C  CB  A GLN A 1 180 ? -22.750 -1.175  14.341  0.70 34.30 ? 180 GLN A CB  1 
ATOM   1262 C  CB  B GLN A 1 180 ? -22.629 -1.354  14.486  0.30 32.55 ? 180 GLN A CB  1 
ATOM   1263 C  CG  A GLN A 1 180 ? -21.505 -2.050  14.525  0.70 43.14 ? 180 GLN A CG  1 
ATOM   1264 C  CG  B GLN A 1 180 ? -21.745 -2.542  14.884  0.30 34.73 ? 180 GLN A CG  1 
ATOM   1265 C  CD  A GLN A 1 180 ? -20.453 -1.511  15.476  0.70 43.43 ? 180 GLN A CD  1 
ATOM   1266 C  CD  B GLN A 1 180 ? -20.622 -2.857  13.912  0.30 36.18 ? 180 GLN A CD  1 
ATOM   1267 O  OE1 A GLN A 1 180 ? -20.249 -2.059  16.561  0.70 51.90 ? 180 GLN A OE1 1 
ATOM   1268 O  OE1 B GLN A 1 180 ? -20.233 -2.032  13.078  0.30 35.15 ? 180 GLN A OE1 1 
ATOM   1269 N  NE2 A GLN A 1 180 ? -19.763 -0.443  15.092  0.70 52.04 ? 180 GLN A NE2 1 
ATOM   1270 N  NE2 B GLN A 1 180 ? -20.063 -4.058  14.022  0.30 35.88 ? 180 GLN A NE2 1 
ATOM   1271 N  N   . PRO A 1 181 ? -24.095 1.568   15.081  1.00 29.70 ? 181 PRO A N   1 
ATOM   1272 C  CA  . PRO A 1 181 ? -25.061 2.559   14.594  1.00 30.57 ? 181 PRO A CA  1 
ATOM   1273 C  C   . PRO A 1 181 ? -25.459 2.272   13.140  1.00 29.04 ? 181 PRO A C   1 
ATOM   1274 O  O   . PRO A 1 181 ? -24.714 1.638   12.400  1.00 28.59 ? 181 PRO A O   1 
ATOM   1275 C  CB  . PRO A 1 181 ? -24.290 3.896   14.735  1.00 30.57 ? 181 PRO A CB  1 
ATOM   1276 C  CG  . PRO A 1 181 ? -23.069 3.565   15.635  1.00 33.47 ? 181 PRO A CG  1 
ATOM   1277 C  CD  . PRO A 1 181 ? -22.748 2.110   15.295  1.00 32.03 ? 181 PRO A CD  1 
ATOM   1278 N  N   . PRO A 1 182 ? -26.602 2.778   12.624  1.00 27.62 ? 182 PRO A N   1 
ATOM   1279 C  CA  . PRO A 1 182 ? -26.870 2.688   11.175  1.00 26.43 ? 182 PRO A CA  1 
ATOM   1280 C  C   . PRO A 1 182 ? -25.785 3.467   10.421  1.00 24.78 ? 182 PRO A C   1 
ATOM   1281 O  O   . PRO A 1 182 ? -25.145 4.366   10.992  1.00 25.60 ? 182 PRO A O   1 
ATOM   1282 C  CB  . PRO A 1 182 ? -28.228 3.383   11.016  1.00 26.13 ? 182 PRO A CB  1 
ATOM   1283 C  CG  . PRO A 1 182 ? -28.825 3.453   12.447  1.00 29.30 ? 182 PRO A CG  1 
ATOM   1284 C  CD  . PRO A 1 182 ? -27.637 3.514   13.383  1.00 29.77 ? 182 PRO A CD  1 
ATOM   1285 N  N   . ARG A 1 183 ? -25.538 3.064   9.171   1.00 24.95 ? 183 ARG A N   1 
ATOM   1286 C  CA  . ARG A 1 183 ? -24.641 3.825   8.315   1.00 25.32 ? 183 ARG A CA  1 
ATOM   1287 C  C   . ARG A 1 183 ? -25.190 3.817   6.891   1.00 26.27 ? 183 ARG A C   1 
ATOM   1288 O  O   . ARG A 1 183 ? -25.852 2.870   6.482   1.00 22.43 ? 183 ARG A O   1 
ATOM   1289 C  CB  . ARG A 1 183 ? -23.202 3.269   8.383   1.00 26.64 ? 183 ARG A CB  1 
ATOM   1290 C  CG  . ARG A 1 183 ? -23.070 1.925   7.641   1.00 27.54 ? 183 ARG A CG  1 
ATOM   1291 C  CD  . ARG A 1 183 ? -21.646 1.329   7.866   1.00 29.06 ? 183 ARG A CD  1 
ATOM   1292 N  NE  . ARG A 1 183 ? -21.540 -0.015  7.271   1.00 30.00 ? 183 ARG A NE  1 
ATOM   1293 C  CZ  . ARG A 1 183 ? -20.417 -0.463  6.719   1.00 29.62 ? 183 ARG A CZ  1 
ATOM   1294 N  NH1 . ARG A 1 183 ? -19.295 0.261   6.772   1.00 31.48 ? 183 ARG A NH1 1 
ATOM   1295 N  NH2 . ARG A 1 183 ? -20.437 -1.632  6.102   1.00 31.40 ? 183 ARG A NH2 1 
ATOM   1296 N  N   . LEU A 1 184 ? -24.767 4.805   6.112   1.00 26.18 ? 184 LEU A N   1 
ATOM   1297 C  CA  . LEU A 1 184 ? -25.129 4.838   4.701   1.00 25.13 ? 184 LEU A CA  1 
ATOM   1298 C  C   . LEU A 1 184 ? -24.436 3.702   3.926   1.00 24.53 ? 184 LEU A C   1 
ATOM   1299 O  O   . LEU A 1 184 ? -23.223 3.471   4.119   1.00 25.99 ? 184 LEU A O   1 
ATOM   1300 C  CB  . LEU A 1 184 ? -24.650 6.176   4.114   1.00 24.97 ? 184 LEU A CB  1 
ATOM   1301 C  CG  . LEU A 1 184 ? -24.949 6.303   2.614   1.00 24.55 ? 184 LEU A CG  1 
ATOM   1302 C  CD1 . LEU A 1 184 ? -26.449 6.473   2.243   1.00 26.77 ? 184 LEU A CD1 1 
ATOM   1303 C  CD2 . LEU A 1 184 ? -24.115 7.572   2.160   1.00 24.10 ? 184 LEU A CD2 1 
ATOM   1304 N  N   . LEU A 1 185 ? -25.211 2.956   3.138   1.00 23.48 ? 185 LEU A N   1 
ATOM   1305 C  CA  . LEU A 1 185 ? -24.698 1.877   2.302   1.00 24.86 ? 185 LEU A CA  1 
ATOM   1306 C  C   . LEU A 1 185 ? -24.669 2.273   0.823   1.00 25.10 ? 185 LEU A C   1 
ATOM   1307 O  O   . LEU A 1 185 ? -23.636 2.122   0.153   1.00 28.54 ? 185 LEU A O   1 
ATOM   1308 C  CB  . LEU A 1 185 ? -25.603 0.657   2.551   1.00 24.56 ? 185 LEU A CB  1 
ATOM   1309 C  CG  . LEU A 1 185 ? -25.142 -0.639  1.873   1.00 24.82 ? 185 LEU A CG  1 
ATOM   1310 C  CD1 . LEU A 1 185 ? -24.015 -1.297  2.759   1.00 24.06 ? 185 LEU A CD1 1 
ATOM   1311 C  CD2 . LEU A 1 185 ? -26.336 -1.664  1.793   1.00 24.72 ? 185 LEU A CD2 1 
ATOM   1312 N  N   . ILE A 1 186 ? -25.807 2.773   0.283   1.00 23.64 ? 186 ILE A N   1 
ATOM   1313 C  CA  . ILE A 1 186 ? -25.895 3.142   -1.122  1.00 26.47 ? 186 ILE A CA  1 
ATOM   1314 C  C   . ILE A 1 186 ? -26.662 4.467   -1.176  1.00 27.16 ? 186 ILE A C   1 
ATOM   1315 O  O   . ILE A 1 186 ? -27.674 4.605   -0.480  1.00 24.77 ? 186 ILE A O   1 
ATOM   1316 C  CB  . ILE A 1 186 ? -26.643 2.026   -1.876  1.00 27.64 ? 186 ILE A CB  1 
ATOM   1317 C  CG1 . ILE A 1 186 ? -25.789 0.735   -1.898  1.00 30.76 ? 186 ILE A CG1 1 
ATOM   1318 C  CG2 . ILE A 1 186 ? -27.054 2.451   -3.291  1.00 26.94 ? 186 ILE A CG2 1 
ATOM   1319 C  CD1 . ILE A 1 186 ? -26.369 -0.367  -2.765  1.00 33.75 ? 186 ILE A CD1 1 
ATOM   1320 N  N   . TYR A 1 187 ? -26.207 5.425   -1.996  1.00 26.57 ? 187 TYR A N   1 
ATOM   1321 C  CA  . TYR A 1 187 ? -26.990 6.657   -2.112  1.00 27.33 ? 187 TYR A CA  1 
ATOM   1322 C  C   . TYR A 1 187 ? -27.489 6.836   -3.543  1.00 26.91 ? 187 TYR A C   1 
ATOM   1323 O  O   . TYR A 1 187 ? -26.885 6.311   -4.476  1.00 26.37 ? 187 TYR A O   1 
ATOM   1324 C  CB  . TYR A 1 187 ? -26.161 7.871   -1.695  1.00 27.94 ? 187 TYR A CB  1 
ATOM   1325 C  CG  . TYR A 1 187 ? -24.860 8.089   -2.464  1.00 27.28 ? 187 TYR A CG  1 
ATOM   1326 C  CD1 . TYR A 1 187 ? -23.695 7.413   -2.108  1.00 30.64 ? 187 TYR A CD1 1 
ATOM   1327 C  CD2 . TYR A 1 187 ? -24.795 8.997   -3.523  1.00 28.16 ? 187 TYR A CD2 1 
ATOM   1328 C  CE1 . TYR A 1 187 ? -22.499 7.622   -2.784  1.00 33.62 ? 187 TYR A CE1 1 
ATOM   1329 C  CE2 . TYR A 1 187 ? -23.601 9.231   -4.182  1.00 27.93 ? 187 TYR A CE2 1 
ATOM   1330 C  CZ  . TYR A 1 187 ? -22.452 8.562   -3.795  1.00 31.39 ? 187 TYR A CZ  1 
ATOM   1331 O  OH  . TYR A 1 187 ? -21.269 8.742   -4.481  1.00 35.04 ? 187 TYR A OH  1 
ATOM   1332 N  N   . ALA A 1 188 ? -28.636 7.524   -3.685  1.00 26.54 ? 188 ALA A N   1 
ATOM   1333 C  CA  . ALA A 1 188 ? -29.250 7.833   -4.962  1.00 27.96 ? 188 ALA A CA  1 
ATOM   1334 C  C   . ALA A 1 188 ? -29.366 6.556   -5.780  1.00 28.47 ? 188 ALA A C   1 
ATOM   1335 O  O   . ALA A 1 188 ? -28.950 6.497   -6.930  1.00 28.07 ? 188 ALA A O   1 
ATOM   1336 C  CB  . ALA A 1 188 ? -28.475 8.935   -5.736  1.00 28.60 ? 188 ALA A CB  1 
ATOM   1337 N  N   . ALA A 1 189 ? -29.918 5.540   -5.113  1.00 26.41 ? 189 ALA A N   1 
ATOM   1338 C  CA  . ALA A 1 189 ? -30.317 4.254   -5.669  1.00 26.57 ? 189 ALA A CA  1 
ATOM   1339 C  C   . ALA A 1 189 ? -29.171 3.314   -6.029  1.00 27.96 ? 189 ALA A C   1 
ATOM   1340 O  O   . ALA A 1 189 ? -29.228 2.113   -5.790  1.00 29.93 ? 189 ALA A O   1 
ATOM   1341 C  CB  . ALA A 1 189 ? -31.317 4.459   -6.801  1.00 25.46 ? 189 ALA A CB  1 
ATOM   1342 N  N   . SER A 1 190 ? -28.076 3.825   -6.577  1.00 28.28 ? 190 SER A N   1 
ATOM   1343 C  CA  . SER A 1 190 ? -27.167 2.874   -7.179  1.00 26.71 ? 190 SER A CA  1 
ATOM   1344 C  C   . SER A 1 190 ? -25.707 3.173   -6.849  1.00 28.69 ? 190 SER A C   1 
ATOM   1345 O  O   . SER A 1 190 ? -24.822 2.470   -7.330  1.00 32.53 ? 190 SER A O   1 
ATOM   1346 C  CB  . SER A 1 190 ? -27.353 2.847   -8.671  1.00 33.25 ? 190 SER A CB  1 
ATOM   1347 O  OG  . SER A 1 190 ? -27.040 4.148   -9.173  1.00 33.20 ? 190 SER A OG  1 
ATOM   1348 N  N   . ASN A 1 191 ? -25.412 4.227   -6.076  1.00 26.07 ? 191 ASN A N   1 
ATOM   1349 C  CA  . ASN A 1 191 ? -24.004 4.509   -5.790  1.00 27.31 ? 191 ASN A CA  1 
ATOM   1350 C  C   . ASN A 1 191 ? -23.526 3.943   -4.455  1.00 28.26 ? 191 ASN A C   1 
ATOM   1351 O  O   . ASN A 1 191 ? -24.085 4.308   -3.410  1.00 29.34 ? 191 ASN A O   1 
ATOM   1352 C  CB  . ASN A 1 191 ? -23.824 6.034   -5.812  1.00 27.49 ? 191 ASN A CB  1 
ATOM   1353 C  CG  . ASN A 1 191 ? -24.292 6.643   -7.111  1.00 33.32 ? 191 ASN A CG  1 
ATOM   1354 O  OD1 . ASN A 1 191 ? -23.578 6.570   -8.111  1.00 38.09 ? 191 ASN A OD1 1 
ATOM   1355 N  ND2 . ASN A 1 191 ? -25.509 7.159   -7.163  1.00 33.52 ? 191 ASN A ND2 1 
ATOM   1356 N  N   . LEU A 1 192 ? -22.391 3.222   -4.456  1.00 29.02 ? 192 LEU A N   1 
ATOM   1357 C  CA  . LEU A 1 192 ? -21.846 2.708   -3.213  1.00 32.37 ? 192 LEU A CA  1 
ATOM   1358 C  C   . LEU A 1 192 ? -21.231 3.859   -2.419  1.00 33.19 ? 192 LEU A C   1 
ATOM   1359 O  O   . LEU A 1 192 ? -20.446 4.626   -2.972  1.00 32.38 ? 192 LEU A O   1 
ATOM   1360 C  CB  . LEU A 1 192 ? -20.787 1.639   -3.426  1.00 32.99 ? 192 LEU A CB  1 
ATOM   1361 C  CG  . LEU A 1 192 ? -21.267 0.330   -4.021  1.00 40.25 ? 192 LEU A CG  1 
ATOM   1362 C  CD1 . LEU A 1 192 ? -20.177 -0.689  -3.760  1.00 42.39 ? 192 LEU A CD1 1 
ATOM   1363 C  CD2 . LEU A 1 192 ? -22.533 -0.043  -3.276  1.00 43.87 ? 192 LEU A CD2 1 
ATOM   1364 N  N   . GLU A 1 193 ? -21.568 3.974   -1.124  1.00 31.85 ? 193 GLU A N   1 
ATOM   1365 C  CA  . GLU A 1 193 ? -20.860 4.915   -0.243  1.00 30.75 ? 193 GLU A CA  1 
ATOM   1366 C  C   . GLU A 1 193 ? -19.378 4.503   -0.151  1.00 31.34 ? 193 GLU A C   1 
ATOM   1367 O  O   . GLU A 1 193 ? -19.051 3.326   -0.318  1.00 30.62 ? 193 GLU A O   1 
ATOM   1368 C  CB  . GLU A 1 193 ? -21.592 4.968   1.119   1.00 30.82 ? 193 GLU A CB  1 
ATOM   1369 C  CG  . GLU A 1 193 ? -20.806 5.503   2.316   1.00 31.91 ? 193 GLU A CG  1 
ATOM   1370 C  CD  . GLU A 1 193 ? -20.536 7.019   2.208   1.00 38.16 ? 193 GLU A CD  1 
ATOM   1371 O  OE1 . GLU A 1 193 ? -20.303 7.517   1.085   1.00 38.97 ? 193 GLU A OE1 1 
ATOM   1372 O  OE2 . GLU A 1 193 ? -20.552 7.703   3.244   1.00 36.17 ? 193 GLU A OE2 1 
ATOM   1373 N  N   . SER A 1 194 ? -18.467 5.462   0.122   1.00 30.52 ? 194 SER A N   1 
ATOM   1374 C  CA  . SER A 1 194 ? -17.045 5.171   0.310   1.00 34.04 ? 194 SER A CA  1 
ATOM   1375 C  C   . SER A 1 194 ? -16.859 4.111   1.375   1.00 33.50 ? 194 SER A C   1 
ATOM   1376 O  O   . SER A 1 194 ? -17.530 4.157   2.420   1.00 32.71 ? 194 SER A O   1 
ATOM   1377 C  CB  . SER A 1 194 ? -16.281 6.399   0.806   1.00 38.82 ? 194 SER A CB  1 
ATOM   1378 O  OG  . SER A 1 194 ? -16.499 7.399   -0.158  1.00 50.20 ? 194 SER A OG  1 
ATOM   1379 N  N   . GLY A 1 195 ? -15.976 3.150   1.065   1.00 36.14 ? 195 GLY A N   1 
ATOM   1380 C  CA  . GLY A 1 195 ? -15.619 2.112   2.012   1.00 33.86 ? 195 GLY A CA  1 
ATOM   1381 C  C   . GLY A 1 195 ? -16.583 0.924   2.014   1.00 37.08 ? 195 GLY A C   1 
ATOM   1382 O  O   . GLY A 1 195 ? -16.333 -0.020  2.752   1.00 40.28 ? 195 GLY A O   1 
ATOM   1383 N  N   . ILE A 1 196 ? -17.706 1.002   1.284   1.00 33.53 ? 196 ILE A N   1 
ATOM   1384 C  CA  . ILE A 1 196 ? -18.631 -0.151  1.174   1.00 31.77 ? 196 ILE A CA  1 
ATOM   1385 C  C   . ILE A 1 196 ? -18.074 -1.153  0.157   1.00 35.81 ? 196 ILE A C   1 
ATOM   1386 O  O   . ILE A 1 196 ? -17.713 -0.763  -0.949  1.00 36.45 ? 196 ILE A O   1 
ATOM   1387 C  CB  . ILE A 1 196 ? -20.072 0.293   0.804   1.00 30.05 ? 196 ILE A CB  1 
ATOM   1388 C  CG1 . ILE A 1 196 ? -20.684 1.239   1.856   1.00 29.73 ? 196 ILE A CG1 1 
ATOM   1389 C  CG2 . ILE A 1 196 ? -20.993 -0.925  0.562   1.00 28.09 ? 196 ILE A CG2 1 
ATOM   1390 C  CD1 . ILE A 1 196 ? -20.563 0.784   3.328   1.00 30.66 ? 196 ILE A CD1 1 
ATOM   1391 N  N   . PRO A 1 197 ? -18.010 -2.473  0.471   1.00 32.58 ? 197 PRO A N   1 
ATOM   1392 C  CA  . PRO A 1 197 ? -17.466 -3.473  -0.451  1.00 34.76 ? 197 PRO A CA  1 
ATOM   1393 C  C   . PRO A 1 197 ? -18.267 -3.649  -1.738  1.00 36.99 ? 197 PRO A C   1 
ATOM   1394 O  O   . PRO A 1 197 ? -19.496 -3.459  -1.780  1.00 33.72 ? 197 PRO A O   1 
ATOM   1395 C  CB  . PRO A 1 197 ? -17.421 -4.800  0.363   1.00 35.22 ? 197 PRO A CB  1 
ATOM   1396 C  CG  . PRO A 1 197 ? -17.818 -4.443  1.776   1.00 42.03 ? 197 PRO A CG  1 
ATOM   1397 C  CD  . PRO A 1 197 ? -18.399 -3.046  1.766   1.00 36.08 ? 197 PRO A CD  1 
ATOM   1398 N  N   . ALA A 1 198 ? -17.569 -4.109  -2.779  1.00 38.02 ? 198 ALA A N   1 
ATOM   1399 C  CA  . ALA A 1 198 ? -18.140 -4.212  -4.106  1.00 37.77 ? 198 ALA A CA  1 
ATOM   1400 C  C   . ALA A 1 198 ? -19.226 -5.283  -4.192  1.00 35.54 ? 198 ALA A C   1 
ATOM   1401 O  O   . ALA A 1 198 ? -19.970 -5.297  -5.153  1.00 37.14 ? 198 ALA A O   1 
ATOM   1402 C  CB  . ALA A 1 198 ? -17.066 -4.496  -5.131  1.00 46.03 ? 198 ALA A CB  1 
ATOM   1403 N  N   . ARG A 1 199 ? -19.333 -6.176  -3.201  1.00 34.48 ? 199 ARG A N   1 
ATOM   1404 C  CA  . ARG A 1 199 ? -20.385 -7.189  -3.251  1.00 31.71 ? 199 ARG A CA  1 
ATOM   1405 C  C   . ARG A 1 199 ? -21.787 -6.579  -3.109  1.00 34.11 ? 199 ARG A C   1 
ATOM   1406 O  O   . ARG A 1 199 ? -22.779 -7.281  -3.340  1.00 32.58 ? 199 ARG A O   1 
ATOM   1407 C  CB  . ARG A 1 199 ? -20.098 -8.306  -2.242  1.00 32.31 ? 199 ARG A CB  1 
ATOM   1408 C  CG  . ARG A 1 199 ? -20.074 -7.809  -0.810  1.00 33.33 ? 199 ARG A CG  1 
ATOM   1409 C  CD  . ARG A 1 199 ? -19.644 -9.004  0.052   1.00 37.53 ? 199 ARG A CD  1 
ATOM   1410 N  NE  . ARG A 1 199 ? -19.650 -8.688  1.480   1.00 35.70 ? 199 ARG A NE  1 
ATOM   1411 C  CZ  . ARG A 1 199 ? -18.649 -8.136  2.129   1.00 36.82 ? 199 ARG A CZ  1 
ATOM   1412 N  NH1 . ARG A 1 199 ? -17.480 -7.925  1.533   1.00 35.22 ? 199 ARG A NH1 1 
ATOM   1413 N  NH2 . ARG A 1 199 ? -18.797 -7.833  3.405   1.00 37.36 ? 199 ARG A NH2 1 
ATOM   1414 N  N   . PHE A 1 200 ? -21.899 -5.319  -2.657  1.00 30.45 ? 200 PHE A N   1 
ATOM   1415 C  CA  . PHE A 1 200 ? -23.206 -4.673  -2.602  1.00 28.08 ? 200 PHE A CA  1 
ATOM   1416 C  C   . PHE A 1 200 ? -23.509 -3.961  -3.921  1.00 30.86 ? 200 PHE A C   1 
ATOM   1417 O  O   . PHE A 1 200 ? -22.622 -3.333  -4.503  1.00 33.94 ? 200 PHE A O   1 
ATOM   1418 C  CB  . PHE A 1 200 ? -23.206 -3.630  -1.463  1.00 26.60 ? 200 PHE A CB  1 
ATOM   1419 C  CG  . PHE A 1 200 ? -23.171 -4.247  -0.073  1.00 28.57 ? 200 PHE A CG  1 
ATOM   1420 C  CD1 . PHE A 1 200 ? -21.951 -4.549  0.546   1.00 31.37 ? 200 PHE A CD1 1 
ATOM   1421 C  CD2 . PHE A 1 200 ? -24.352 -4.547  0.609   1.00 27.76 ? 200 PHE A CD2 1 
ATOM   1422 C  CE1 . PHE A 1 200 ? -21.891 -5.108  1.842   1.00 30.42 ? 200 PHE A CE1 1 
ATOM   1423 C  CE2 . PHE A 1 200 ? -24.289 -5.119  1.873   1.00 28.70 ? 200 PHE A CE2 1 
ATOM   1424 C  CZ  . PHE A 1 200 ? -23.076 -5.384  2.486   1.00 28.66 ? 200 PHE A CZ  1 
ATOM   1425 N  N   . SER A 1 201 ? -24.774 -3.980  -4.364  1.00 30.00 ? 201 SER A N   1 
ATOM   1426 C  CA  . SER A 1 201 ? -25.176 -3.156  -5.491  1.00 30.15 ? 201 SER A CA  1 
ATOM   1427 C  C   . SER A 1 201 ? -26.637 -2.756  -5.353  1.00 31.47 ? 201 SER A C   1 
ATOM   1428 O  O   . SER A 1 201 ? -27.422 -3.422  -4.680  1.00 32.40 ? 201 SER A O   1 
ATOM   1429 C  CB  . SER A 1 201 ? -24.941 -3.832  -6.846  1.00 31.98 ? 201 SER A CB  1 
ATOM   1430 O  OG  . SER A 1 201 ? -25.731 -5.015  -6.855  1.00 39.76 ? 201 SER A OG  1 
ATOM   1431 N  N   . GLY A 1 202 ? -26.968 -1.648  -6.004  1.00 28.43 ? 202 GLY A N   1 
ATOM   1432 C  CA  . GLY A 1 202 ? -28.318 -1.118  -5.925  1.00 29.68 ? 202 GLY A CA  1 
ATOM   1433 C  C   . GLY A 1 202 ? -28.793 -0.789  -7.321  1.00 29.39 ? 202 GLY A C   1 
ATOM   1434 O  O   . GLY A 1 202 ? -27.990 -0.379  -8.159  1.00 29.96 ? 202 GLY A O   1 
ATOM   1435 N  N   . SER A 1 203 ? -30.087 -1.026  -7.568  1.00 27.23 ? 203 SER A N   1 
ATOM   1436 C  CA  . SER A 1 203 ? -30.668 -0.665  -8.836  1.00 29.62 ? 203 SER A CA  1 
ATOM   1437 C  C   . SER A 1 203 ? -32.029 -0.008  -8.600  1.00 30.37 ? 203 SER A C   1 
ATOM   1438 O  O   . SER A 1 203 ? -32.608 -0.086  -7.503  1.00 29.54 ? 203 SER A O   1 
ATOM   1439 C  CB  . SER A 1 203 ? -30.772 -1.935  -9.696  1.00 31.83 ? 203 SER A CB  1 
ATOM   1440 O  OG  . SER A 1 203 ? -31.734 -2.846  -9.155  1.00 33.12 ? 203 SER A OG  1 
ATOM   1441 N  N   . GLY A 1 204 ? -32.603 0.538   -9.678  1.00 30.91 ? 204 GLY A N   1 
ATOM   1442 C  CA  . GLY A 1 204 ? -34.006 0.924   -9.658  1.00 32.22 ? 204 GLY A CA  1 
ATOM   1443 C  C   . GLY A 1 204 ? -34.175 2.400   -10.041 1.00 30.17 ? 204 GLY A C   1 
ATOM   1444 O  O   . GLY A 1 204 ? -33.205 3.117   -10.273 1.00 32.74 ? 204 GLY A O   1 
ATOM   1445 N  N   . SER A 1 205 ? -35.434 2.811   -10.181 1.00 32.02 ? 205 SER A N   1 
ATOM   1446 C  CA  . SER A 1 205 ? -35.780 4.194   -10.461 1.00 33.94 ? 205 SER A CA  1 
ATOM   1447 C  C   . SER A 1 205 ? -37.274 4.310   -10.209 1.00 32.81 ? 205 SER A C   1 
ATOM   1448 O  O   . SER A 1 205 ? -37.976 3.290   -10.168 1.00 33.72 ? 205 SER A O   1 
ATOM   1449 C  CB  . SER A 1 205 ? -35.494 4.551   -11.927 1.00 36.45 ? 205 SER A CB  1 
ATOM   1450 O  OG  . SER A 1 205 ? -36.230 3.680   -12.771 1.00 36.52 ? 205 SER A OG  1 
ATOM   1451 N  N   . GLY A 1 206 ? -37.733 5.544   -10.033 1.00 35.21 ? 206 GLY A N   1 
ATOM   1452 C  CA  . GLY A 1 206 ? -39.160 5.786   -9.983  1.00 35.31 ? 206 GLY A CA  1 
ATOM   1453 C  C   . GLY A 1 206 ? -39.717 5.366   -8.626  1.00 33.50 ? 206 GLY A C   1 
ATOM   1454 O  O   . GLY A 1 206 ? -39.494 6.044   -7.634  1.00 31.85 ? 206 GLY A O   1 
ATOM   1455 N  N   . THR A 1 207 ? -40.472 4.250   -8.618  1.00 33.24 ? 207 THR A N   1 
ATOM   1456 C  CA  . THR A 1 207 ? -41.010 3.705   -7.374  1.00 32.29 ? 207 THR A CA  1 
ATOM   1457 C  C   . THR A 1 207 ? -40.339 2.379   -6.965  1.00 32.05 ? 207 THR A C   1 
ATOM   1458 O  O   . THR A 1 207 ? -40.659 1.912   -5.892  1.00 36.88 ? 207 THR A O   1 
ATOM   1459 C  CB  . THR A 1 207 ? -42.527 3.522   -7.469  1.00 35.68 ? 207 THR A CB  1 
ATOM   1460 O  OG1 . THR A 1 207 ? -42.720 2.651   -8.599  1.00 33.92 ? 207 THR A OG1 1 
ATOM   1461 C  CG2 . THR A 1 207 ? -43.294 4.818   -7.668  1.00 34.66 ? 207 THR A CG2 1 
ATOM   1462 N  N   . ASP A 1 208 ? -39.555 1.696   -7.821  1.00 30.18 ? 208 ASP A N   1 
ATOM   1463 C  CA  A ASP A 1 208 ? -39.097 0.343   -7.517  0.60 32.37 ? 208 ASP A CA  1 
ATOM   1464 C  CA  B ASP A 1 208 ? -39.094 0.354   -7.493  0.40 30.68 ? 208 ASP A CA  1 
ATOM   1465 C  C   . ASP A 1 208 ? -37.574 0.321   -7.441  1.00 30.76 ? 208 ASP A C   1 
ATOM   1466 O  O   . ASP A 1 208 ? -36.900 0.735   -8.405  1.00 32.05 ? 208 ASP A O   1 
ATOM   1467 C  CB  A ASP A 1 208 ? -39.440 -0.657  -8.610  0.60 36.62 ? 208 ASP A CB  1 
ATOM   1468 C  CB  B ASP A 1 208 ? -39.649 -0.676  -8.459  0.40 31.28 ? 208 ASP A CB  1 
ATOM   1469 C  CG  A ASP A 1 208 ? -40.831 -0.569  -9.219  0.60 42.75 ? 208 ASP A CG  1 
ATOM   1470 C  CG  B ASP A 1 208 ? -41.158 -0.827  -8.391  0.40 32.09 ? 208 ASP A CG  1 
ATOM   1471 O  OD1 A ASP A 1 208 ? -41.796 -0.457  -8.448  0.60 46.40 ? 208 ASP A OD1 1 
ATOM   1472 O  OD1 B ASP A 1 208 ? -41.842 0.223   -8.408  0.40 33.59 ? 208 ASP A OD1 1 
ATOM   1473 O  OD2 A ASP A 1 208 ? -40.935 -0.655  -10.469 0.60 48.40 ? 208 ASP A OD2 1 
ATOM   1474 O  OD2 B ASP A 1 208 ? -41.627 -1.979  -8.332  0.40 34.13 ? 208 ASP A OD2 1 
ATOM   1475 N  N   . PHE A 1 209 ? -37.047 -0.238  -6.323  1.00 28.26 ? 209 PHE A N   1 
ATOM   1476 C  CA  . PHE A 1 209 ? -35.617 -0.273  -6.053  1.00 26.21 ? 209 PHE A CA  1 
ATOM   1477 C  C   . PHE A 1 209 ? -35.261 -1.657  -5.523  1.00 28.50 ? 209 PHE A C   1 
ATOM   1478 O  O   . PHE A 1 209 ? -36.118 -2.319  -4.862  1.00 28.28 ? 209 PHE A O   1 
ATOM   1479 C  CB  . PHE A 1 209 ? -35.203 0.828   -5.056  1.00 28.23 ? 209 PHE A CB  1 
ATOM   1480 C  CG  . PHE A 1 209 ? -35.570 2.175   -5.666  1.00 27.59 ? 209 PHE A CG  1 
ATOM   1481 C  CD1 . PHE A 1 209 ? -34.649 2.859   -6.476  1.00 26.14 ? 209 PHE A CD1 1 
ATOM   1482 C  CD2 . PHE A 1 209 ? -36.834 2.728   -5.464  1.00 28.48 ? 209 PHE A CD2 1 
ATOM   1483 C  CE1 . PHE A 1 209 ? -35.001 4.076   -7.043  1.00 28.60 ? 209 PHE A CE1 1 
ATOM   1484 C  CE2 . PHE A 1 209 ? -37.194 3.948   -6.060  1.00 29.29 ? 209 PHE A CE2 1 
ATOM   1485 C  CZ  . PHE A 1 209 ? -36.270 4.621   -6.843  1.00 28.20 ? 209 PHE A CZ  1 
ATOM   1486 N  N   . THR A 1 210 ? -33.991 -2.050  -5.716  1.00 28.41 ? 210 THR A N   1 
ATOM   1487 C  CA  . THR A 1 210 ? -33.542 -3.377  -5.306  1.00 27.88 ? 210 THR A CA  1 
ATOM   1488 C  C   . THR A 1 210 ? -32.123 -3.286  -4.771  1.00 29.39 ? 210 THR A C   1 
ATOM   1489 O  O   . THR A 1 210 ? -31.256 -2.764  -5.467  1.00 27.92 ? 210 THR A O   1 
ATOM   1490 C  CB  . THR A 1 210 ? -33.605 -4.379  -6.469  1.00 28.32 ? 210 THR A CB  1 
ATOM   1491 O  OG1 . THR A 1 210 ? -34.915 -4.310  -7.028  1.00 28.22 ? 210 THR A OG1 1 
ATOM   1492 C  CG2 . THR A 1 210 ? -33.426 -5.823  -6.016  1.00 27.97 ? 210 THR A CG2 1 
ATOM   1493 N  N   . LEU A 1 211 ? -31.877 -3.887  -3.604  1.00 27.17 ? 211 LEU A N   1 
ATOM   1494 C  CA  . LEU A 1 211 ? -30.525 -4.058  -3.083  1.00 26.15 ? 211 LEU A CA  1 
ATOM   1495 C  C   . LEU A 1 211 ? -30.097 -5.497  -3.360  1.00 27.88 ? 211 LEU A C   1 
ATOM   1496 O  O   . LEU A 1 211 ? -30.861 -6.421  -3.096  1.00 27.58 ? 211 LEU A O   1 
ATOM   1497 C  CB  . LEU A 1 211 ? -30.585 -3.768  -1.578  1.00 25.26 ? 211 LEU A CB  1 
ATOM   1498 C  CG  . LEU A 1 211 ? -29.275 -4.002  -0.820  1.00 25.70 ? 211 LEU A CG  1 
ATOM   1499 C  CD1 . LEU A 1 211 ? -28.186 -2.982  -1.242  1.00 26.23 ? 211 LEU A CD1 1 
ATOM   1500 C  CD2 . LEU A 1 211 ? -29.453 -3.894  0.700   1.00 27.00 ? 211 LEU A CD2 1 
ATOM   1501 N  N   . ASN A 1 212 ? -28.858 -5.693  -3.802  1.00 26.87 ? 212 ASN A N   1 
ATOM   1502 C  CA  . ASN A 1 212 ? -28.314 -7.027  -4.016  1.00 30.43 ? 212 ASN A CA  1 
ATOM   1503 C  C   . ASN A 1 212 ? -27.010 -7.135  -3.259  1.00 30.90 ? 212 ASN A C   1 
ATOM   1504 O  O   . ASN A 1 212 ? -26.222 -6.198  -3.270  1.00 28.61 ? 212 ASN A O   1 
ATOM   1505 C  CB  . ASN A 1 212 ? -28.059 -7.328  -5.495  1.00 27.65 ? 212 ASN A CB  1 
ATOM   1506 C  CG  . ASN A 1 212 ? -29.248 -8.077  -6.063  1.00 29.79 ? 212 ASN A CG  1 
ATOM   1507 O  OD1 . ASN A 1 212 ? -29.299 -9.308  -5.917  1.00 29.28 ? 212 ASN A OD1 1 
ATOM   1508 N  ND2 . ASN A 1 212 ? -30.175 -7.387  -6.723  1.00 27.27 ? 212 ASN A ND2 1 
ATOM   1509 N  N   . ILE A 1 213 ? -26.787 -8.307  -2.671  1.00 28.26 ? 213 ILE A N   1 
ATOM   1510 C  CA  . ILE A 1 213 ? -25.539 -8.603  -1.979  1.00 28.33 ? 213 ILE A CA  1 
ATOM   1511 C  C   . ILE A 1 213 ? -25.079 -9.986  -2.430  1.00 30.84 ? 213 ILE A C   1 
ATOM   1512 O  O   . ILE A 1 213 ? -25.814 -10.958 -2.256  1.00 29.17 ? 213 ILE A O   1 
ATOM   1513 C  CB  . ILE A 1 213 ? -25.726 -8.587  -0.443  1.00 27.43 ? 213 ILE A CB  1 
ATOM   1514 C  CG1 . ILE A 1 213 ? -26.658 -7.449  0.049   1.00 28.98 ? 213 ILE A CG1 1 
ATOM   1515 C  CG2 . ILE A 1 213 ? -24.362 -8.620  0.257   1.00 28.62 ? 213 ILE A CG2 1 
ATOM   1516 C  CD1 . ILE A 1 213 ? -26.924 -7.481  1.557   1.00 28.62 ? 213 ILE A CD1 1 
ATOM   1517 N  N   . HIS A 1 214 ? -23.887 -10.071 -3.039  1.00 30.76 ? 214 HIS A N   1 
ATOM   1518 C  CA  . HIS A 1 214 ? -23.416 -11.384 -3.488  1.00 32.20 ? 214 HIS A CA  1 
ATOM   1519 C  C   . HIS A 1 214 ? -21.926 -11.289 -3.766  1.00 35.00 ? 214 HIS A C   1 
ATOM   1520 O  O   . HIS A 1 214 ? -21.497 -10.326 -4.396  1.00 33.92 ? 214 HIS A O   1 
ATOM   1521 C  CB  . HIS A 1 214 ? -24.103 -11.851 -4.780  1.00 33.02 ? 214 HIS A CB  1 
ATOM   1522 C  CG  . HIS A 1 214 ? -23.499 -13.124 -5.341  1.00 38.17 ? 214 HIS A CG  1 
ATOM   1523 N  ND1 . HIS A 1 214 ? -22.453 -13.125 -6.247  1.00 38.63 ? 214 HIS A ND1 1 
ATOM   1524 C  CD2 . HIS A 1 214 ? -23.759 -14.434 -5.068  1.00 36.61 ? 214 HIS A CD2 1 
ATOM   1525 C  CE1 . HIS A 1 214 ? -22.097 -14.381 -6.501  1.00 41.82 ? 214 HIS A CE1 1 
ATOM   1526 N  NE2 . HIS A 1 214 ? -22.896 -15.191 -5.819  1.00 39.05 ? 214 HIS A NE2 1 
ATOM   1527 N  N   . PRO A 1 215 ? -21.081 -12.230 -3.290  1.00 38.18 ? 215 PRO A N   1 
ATOM   1528 C  CA  . PRO A 1 215 ? -21.488 -13.314 -2.380  1.00 36.80 ? 215 PRO A CA  1 
ATOM   1529 C  C   . PRO A 1 215 ? -21.616 -12.829 -0.927  1.00 35.97 ? 215 PRO A C   1 
ATOM   1530 O  O   . PRO A 1 215 ? -20.750 -12.074 -0.445  1.00 36.60 ? 215 PRO A O   1 
ATOM   1531 C  CB  . PRO A 1 215 ? -20.318 -14.356 -2.538  1.00 39.38 ? 215 PRO A CB  1 
ATOM   1532 C  CG  . PRO A 1 215 ? -19.405 -13.771 -3.625  1.00 43.25 ? 215 PRO A CG  1 
ATOM   1533 C  CD  . PRO A 1 215 ? -19.637 -12.260 -3.594  1.00 39.43 ? 215 PRO A CD  1 
ATOM   1534 N  N   . VAL A 1 216 ? -22.710 -13.223 -0.240  1.00 34.27 ? 216 VAL A N   1 
ATOM   1535 C  CA  . VAL A 1 216 ? -22.917 -12.847 1.154   1.00 32.90 ? 216 VAL A CA  1 
ATOM   1536 C  C   . VAL A 1 216 ? -21.765 -13.360 2.030   1.00 36.95 ? 216 VAL A C   1 
ATOM   1537 O  O   . VAL A 1 216 ? -21.339 -14.513 1.903   1.00 36.27 ? 216 VAL A O   1 
ATOM   1538 C  CB  . VAL A 1 216 ? -24.281 -13.314 1.691   1.00 34.92 ? 216 VAL A CB  1 
ATOM   1539 C  CG1 . VAL A 1 216 ? -24.341 -13.243 3.212   1.00 40.12 ? 216 VAL A CG1 1 
ATOM   1540 C  CG2 . VAL A 1 216 ? -25.410 -12.479 1.088   1.00 31.12 ? 216 VAL A CG2 1 
ATOM   1541 N  N   . GLU A 1 217 ? -21.265 -12.487 2.918   1.00 33.15 ? 217 GLU A N   1 
ATOM   1542 C  CA  . GLU A 1 217 ? -20.303 -12.850 3.957   1.00 34.96 ? 217 GLU A CA  1 
ATOM   1543 C  C   . GLU A 1 217 ? -20.927 -12.659 5.339   1.00 34.33 ? 217 GLU A C   1 
ATOM   1544 O  O   . GLU A 1 217 ? -21.931 -11.984 5.497   1.00 33.22 ? 217 GLU A O   1 
ATOM   1545 C  CB  . GLU A 1 217 ? -19.072 -11.942 3.877   1.00 36.67 ? 217 GLU A CB  1 
ATOM   1546 C  CG  . GLU A 1 217 ? -18.353 -12.099 2.538   1.00 44.33 ? 217 GLU A CG  1 
ATOM   1547 C  CD  . GLU A 1 217 ? -17.014 -11.390 2.458   1.00 47.87 ? 217 GLU A CD  1 
ATOM   1548 O  OE1 . GLU A 1 217 ? -16.548 -10.824 3.465   1.00 56.44 ? 217 GLU A OE1 1 
ATOM   1549 O  OE2 . GLU A 1 217 ? -16.437 -11.409 1.365   1.00 56.35 ? 217 GLU A OE2 1 
ATOM   1550 N  N   . GLU A 1 218 ? -20.306 -13.235 6.371   1.00 37.85 ? 218 GLU A N   1 
ATOM   1551 C  CA  . GLU A 1 218 ? -20.798 -13.152 7.745   1.00 35.67 ? 218 GLU A CA  1 
ATOM   1552 C  C   . GLU A 1 218 ? -21.001 -11.703 8.214   1.00 34.99 ? 218 GLU A C   1 
ATOM   1553 O  O   . GLU A 1 218 ? -21.969 -11.423 8.912   1.00 34.94 ? 218 GLU A O   1 
ATOM   1554 C  CB  . GLU A 1 218 ? -19.752 -13.835 8.638   1.00 41.81 ? 218 GLU A CB  1 
ATOM   1555 C  CG  . GLU A 1 218 ? -20.295 -14.304 9.980   0.60 46.16 ? 218 GLU A CG  1 
ATOM   1556 C  CD  . GLU A 1 218 ? -19.312 -15.347 10.477  0.60 53.10 ? 218 GLU A CD  1 
ATOM   1557 O  OE1 . GLU A 1 218 ? -19.622 -16.550 10.330  0.60 57.92 ? 218 GLU A OE1 1 
ATOM   1558 O  OE2 . GLU A 1 218 ? -18.233 -14.963 10.964  0.60 54.26 ? 218 GLU A OE2 1 
ATOM   1559 N  N   . GLU A 1 219 ? -20.076 -10.806 7.848   1.00 34.30 ? 219 GLU A N   1 
ATOM   1560 C  CA  A GLU A 1 219 ? -20.137 -9.387  8.180   0.50 32.53 ? 219 GLU A CA  1 
ATOM   1561 C  CA  B GLU A 1 219 ? -20.173 -9.402  8.230   0.50 32.28 ? 219 GLU A CA  1 
ATOM   1562 C  C   . GLU A 1 219 ? -21.419 -8.748  7.628   1.00 32.17 ? 219 GLU A C   1 
ATOM   1563 O  O   . GLU A 1 219 ? -21.783 -7.647  8.024   1.00 34.46 ? 219 GLU A O   1 
ATOM   1564 C  CB  A GLU A 1 219 ? -18.799 -8.674  7.884   0.50 39.68 ? 219 GLU A CB  1 
ATOM   1565 C  CB  B GLU A 1 219 ? -18.965 -8.578  7.763   0.50 38.86 ? 219 GLU A CB  1 
ATOM   1566 C  CG  A GLU A 1 219 ? -18.451 -8.289  6.440   0.50 42.80 ? 219 GLU A CG  1 
ATOM   1567 C  CG  B GLU A 1 219 ? -17.874 -8.371  8.817   0.50 42.80 ? 219 GLU A CG  1 
ATOM   1568 C  CD  A GLU A 1 219 ? -17.044 -7.747  6.074   0.50 45.46 ? 219 GLU A CD  1 
ATOM   1569 C  CD  B GLU A 1 219 ? -18.139 -7.569  10.082  0.50 41.78 ? 219 GLU A CD  1 
ATOM   1570 O  OE1 A GLU A 1 219 ? -16.098 -8.436  6.500   0.50 50.10 ? 219 GLU A OE1 1 
ATOM   1571 O  OE1 B GLU A 1 219 ? -18.332 -6.315  10.063  0.50 39.68 ? 219 GLU A OE1 1 
ATOM   1572 O  OE2 A GLU A 1 219 ? -16.823 -6.723  5.341   0.50 38.86 ? 219 GLU A OE2 1 
ATOM   1573 O  OE2 B GLU A 1 219 ? -18.108 -8.246  11.136  0.50 48.62 ? 219 GLU A OE2 1 
ATOM   1574 N  N   . ASP A 1 220 ? -22.125 -9.400  6.696   1.00 31.09 ? 220 ASP A N   1 
ATOM   1575 C  CA  . ASP A 1 220 ? -23.250 -8.720  6.043   1.00 27.69 ? 220 ASP A CA  1 
ATOM   1576 C  C   . ASP A 1 220 ? -24.560 -8.918  6.792   1.00 26.40 ? 220 ASP A C   1 
ATOM   1577 O  O   . ASP A 1 220 ? -25.604 -8.355  6.404   1.00 28.80 ? 220 ASP A O   1 
ATOM   1578 C  CB  . ASP A 1 220 ? -23.427 -9.194  4.608   1.00 27.49 ? 220 ASP A CB  1 
ATOM   1579 C  CG  . ASP A 1 220 ? -22.189 -8.934  3.763   1.00 33.77 ? 220 ASP A CG  1 
ATOM   1580 O  OD1 . ASP A 1 220 ? -21.458 -7.912  4.039   1.00 34.55 ? 220 ASP A OD1 1 
ATOM   1581 O  OD2 . ASP A 1 220 ? -21.874 -9.790  2.913   1.00 35.80 ? 220 ASP A OD2 1 
ATOM   1582 N  N   . ALA A 1 221 ? -24.533 -9.721  7.861   1.00 29.18 ? 221 ALA A N   1 
ATOM   1583 C  CA  . ALA A 1 221 ? -25.715 -9.869  8.697   1.00 30.27 ? 221 ALA A CA  1 
ATOM   1584 C  C   . ALA A 1 221 ? -26.059 -8.528  9.362   1.00 30.50 ? 221 ALA A C   1 
ATOM   1585 O  O   . ALA A 1 221 ? -25.230 -7.960  10.070  1.00 30.49 ? 221 ALA A O   1 
ATOM   1586 C  CB  . ALA A 1 221 ? -25.472 -10.950 9.724   1.00 32.20 ? 221 ALA A CB  1 
ATOM   1587 N  N   . ALA A 1 222 ? -27.253 -7.987  9.085   1.00 25.96 ? 222 ALA A N   1 
ATOM   1588 C  CA  . ALA A 1 222 ? -27.552 -6.623  9.543   1.00 26.51 ? 222 ALA A CA  1 
ATOM   1589 C  C   . ALA A 1 222 ? -29.022 -6.380  9.253   1.00 28.96 ? 222 ALA A C   1 
ATOM   1590 O  O   . ALA A 1 222 ? -29.669 -7.228  8.618   1.00 31.05 ? 222 ALA A O   1 
ATOM   1591 C  CB  . ALA A 1 222 ? -26.684 -5.617  8.756   1.00 27.58 ? 222 ALA A CB  1 
ATOM   1592 N  N   . THR A 1 223 ? -29.552 -5.226  9.669   1.00 26.75 ? 223 THR A N   1 
ATOM   1593 C  CA  . THR A 1 223 ? -30.853 -4.812  9.162   1.00 27.62 ? 223 THR A CA  1 
ATOM   1594 C  C   . THR A 1 223 ? -30.631 -3.718  8.117   1.00 23.97 ? 223 THR A C   1 
ATOM   1595 O  O   . THR A 1 223 ? -29.801 -2.804  8.350   1.00 25.55 ? 223 THR A O   1 
ATOM   1596 C  CB  . THR A 1 223 ? -31.664 -4.312  10.361  1.00 29.07 ? 223 THR A CB  1 
ATOM   1597 O  OG1 . THR A 1 223 ? -31.899 -5.427  11.212  1.00 32.37 ? 223 THR A OG1 1 
ATOM   1598 C  CG2 . THR A 1 223 ? -33.038 -3.831  9.926   1.00 25.97 ? 223 THR A CG2 1 
ATOM   1599 N  N   . TYR A 1 224 ? -31.371 -3.820  7.002   1.00 23.86 ? 224 TYR A N   1 
ATOM   1600 C  CA  . TYR A 1 224 ? -31.217 -2.924  5.872   1.00 23.94 ? 224 TYR A CA  1 
ATOM   1601 C  C   . TYR A 1 224 ? -32.479 -2.072  5.843   1.00 23.51 ? 224 TYR A C   1 
ATOM   1602 O  O   . TYR A 1 224 ? -33.562 -2.628  5.938   1.00 25.29 ? 224 TYR A O   1 
ATOM   1603 C  CB  . TYR A 1 224 ? -31.018 -3.748  4.584   1.00 23.02 ? 224 TYR A CB  1 
ATOM   1604 C  CG  . TYR A 1 224 ? -29.641 -4.391  4.671   1.00 22.12 ? 224 TYR A CG  1 
ATOM   1605 C  CD1 . TYR A 1 224 ? -28.502 -3.749  4.187   1.00 21.50 ? 224 TYR A CD1 1 
ATOM   1606 C  CD2 . TYR A 1 224 ? -29.491 -5.695  5.147   1.00 24.81 ? 224 TYR A CD2 1 
ATOM   1607 C  CE1 . TYR A 1 224 ? -27.243 -4.308  4.296   1.00 24.50 ? 224 TYR A CE1 1 
ATOM   1608 C  CE2 . TYR A 1 224 ? -28.230 -6.266  5.258   1.00 24.99 ? 224 TYR A CE2 1 
ATOM   1609 C  CZ  . TYR A 1 224 ? -27.116 -5.608  4.754   1.00 25.84 ? 224 TYR A CZ  1 
ATOM   1610 O  OH  . TYR A 1 224 ? -25.862 -6.164  4.887   1.00 25.74 ? 224 TYR A OH  1 
ATOM   1611 N  N   . TYR A 1 225 ? -32.322 -0.726  5.739   1.00 22.87 ? 225 TYR A N   1 
ATOM   1612 C  CA  . TYR A 1 225 ? -33.479 0.127   5.552   1.00 23.45 ? 225 TYR A CA  1 
ATOM   1613 C  C   . TYR A 1 225 ? -33.335 0.970   4.284   1.00 24.72 ? 225 TYR A C   1 
ATOM   1614 O  O   . TYR A 1 225 ? -32.243 1.503   4.009   1.00 27.21 ? 225 TYR A O   1 
ATOM   1615 C  CB  . TYR A 1 225 ? -33.553 1.185   6.677   1.00 23.10 ? 225 TYR A CB  1 
ATOM   1616 C  CG  . TYR A 1 225 ? -33.764 0.619   8.081   1.00 24.23 ? 225 TYR A CG  1 
ATOM   1617 C  CD1 . TYR A 1 225 ? -35.042 0.279   8.548   1.00 23.67 ? 225 TYR A CD1 1 
ATOM   1618 C  CD2 . TYR A 1 225 ? -32.680 0.418   8.933   1.00 25.19 ? 225 TYR A CD2 1 
ATOM   1619 C  CE1 . TYR A 1 225 ? -35.243 -0.214  9.842   1.00 25.37 ? 225 TYR A CE1 1 
ATOM   1620 C  CE2 . TYR A 1 225 ? -32.864 -0.076  10.227  1.00 27.07 ? 225 TYR A CE2 1 
ATOM   1621 C  CZ  . TYR A 1 225 ? -34.139 -0.414  10.667  1.00 27.17 ? 225 TYR A CZ  1 
ATOM   1622 O  OH  . TYR A 1 225 ? -34.311 -0.826  11.968  1.00 29.41 ? 225 TYR A OH  1 
ATOM   1623 N  N   . CYS A 1 226 ? -34.454 1.163   3.538   1.00 25.49 ? 226 CYS A N   1 
ATOM   1624 C  CA  . CYS A 1 226 ? -34.442 2.132   2.443   1.00 26.16 ? 226 CYS A CA  1 
ATOM   1625 C  C   . CYS A 1 226 ? -35.023 3.432   2.995   1.00 26.17 ? 226 CYS A C   1 
ATOM   1626 O  O   . CYS A 1 226 ? -35.699 3.436   4.049   1.00 25.35 ? 226 CYS A O   1 
ATOM   1627 C  CB  . CYS A 1 226 ? -35.241 1.630   1.233   1.00 26.46 ? 226 CYS A CB  1 
ATOM   1628 S  SG  . CYS A 1 226 ? -36.908 1.041   1.691   1.00 31.04 ? 226 CYS A SG  1 
ATOM   1629 N  N   . GLN A 1 227 ? -34.736 4.540   2.287   1.00 23.96 ? 227 GLN A N   1 
ATOM   1630 C  CA  . GLN A 1 227 ? -35.168 5.853   2.735   1.00 25.89 ? 227 GLN A CA  1 
ATOM   1631 C  C   . GLN A 1 227 ? -35.419 6.700   1.494   1.00 26.26 ? 227 GLN A C   1 
ATOM   1632 O  O   . GLN A 1 227 ? -34.613 6.622   0.564   1.00 26.86 ? 227 GLN A O   1 
ATOM   1633 C  CB  . GLN A 1 227 ? -34.008 6.508   3.505   1.00 26.23 ? 227 GLN A CB  1 
ATOM   1634 C  CG  . GLN A 1 227 ? -34.380 7.903   3.979   1.00 25.75 ? 227 GLN A CG  1 
ATOM   1635 C  CD  . GLN A 1 227 ? -33.637 9.041   3.286   1.00 35.00 ? 227 GLN A CD  1 
ATOM   1636 O  OE1 . GLN A 1 227 ? -33.419 10.091  3.897   1.00 36.86 ? 227 GLN A OE1 1 
ATOM   1637 N  NE2 . GLN A 1 227 ? -33.296 8.893   2.011   1.00 32.32 ? 227 GLN A NE2 1 
ATOM   1638 N  N   . GLN A 1 228 ? -36.463 7.527   1.506   1.00 27.08 ? 228 GLN A N   1 
ATOM   1639 C  CA  . GLN A 1 228 ? -36.578 8.533   0.465   1.00 25.74 ? 228 GLN A CA  1 
ATOM   1640 C  C   . GLN A 1 228 ? -36.424 9.927   1.048   1.00 27.18 ? 228 GLN A C   1 
ATOM   1641 O  O   . GLN A 1 228 ? -36.919 10.183  2.141   1.00 25.30 ? 228 GLN A O   1 
ATOM   1642 C  CB  . GLN A 1 228 ? -37.883 8.433   -0.318  1.00 25.87 ? 228 GLN A CB  1 
ATOM   1643 C  CG  . GLN A 1 228 ? -39.156 8.757   0.459   1.00 27.18 ? 228 GLN A CG  1 
ATOM   1644 C  CD  . GLN A 1 228 ? -39.446 10.236  0.531   1.00 26.92 ? 228 GLN A CD  1 
ATOM   1645 O  OE1 . GLN A 1 228 ? -39.086 10.997  -0.369  1.00 29.46 ? 228 GLN A OE1 1 
ATOM   1646 N  NE2 . GLN A 1 228 ? -40.060 10.674  1.603   1.00 27.79 ? 228 GLN A NE2 1 
ATOM   1647 N  N   . ASN A 1 229 ? -35.837 10.812  0.224   1.00 26.05 ? 229 ASN A N   1 
ATOM   1648 C  CA  . ASN A 1 229 ? -35.707 12.209  0.637   1.00 27.67 ? 229 ASN A CA  1 
ATOM   1649 C  C   . ASN A 1 229 ? -36.089 13.139  -0.526  1.00 30.63 ? 229 ASN A C   1 
ATOM   1650 O  O   . ASN A 1 229 ? -35.569 14.258  -0.623  1.00 30.38 ? 229 ASN A O   1 
ATOM   1651 C  CB  . ASN A 1 229 ? -34.356 12.537  1.297   1.00 28.72 ? 229 ASN A CB  1 
ATOM   1652 C  CG  . ASN A 1 229 ? -33.165 12.405  0.375   1.00 34.82 ? 229 ASN A CG  1 
ATOM   1653 O  OD1 . ASN A 1 229 ? -32.903 11.301  -0.122  1.00 34.54 ? 229 ASN A OD1 1 
ATOM   1654 N  ND2 . ASN A 1 229 ? -32.448 13.500  0.076   1.00 33.50 ? 229 ASN A ND2 1 
ATOM   1655 N  N   . ASN A 1 230 ? -36.960 12.656  -1.412  1.00 28.79 ? 230 ASN A N   1 
ATOM   1656 C  CA  . ASN A 1 230 ? -37.537 13.473  -2.483  1.00 32.46 ? 230 ASN A CA  1 
ATOM   1657 C  C   . ASN A 1 230 ? -38.561 14.477  -1.936  1.00 35.19 ? 230 ASN A C   1 
ATOM   1658 O  O   . ASN A 1 230 ? -38.679 15.586  -2.468  1.00 36.88 ? 230 ASN A O   1 
ATOM   1659 C  CB  . ASN A 1 230 ? -38.173 12.595  -3.557  1.00 32.04 ? 230 ASN A CB  1 
ATOM   1660 C  CG  . ASN A 1 230 ? -38.439 13.360  -4.833  1.00 34.67 ? 230 ASN A CG  1 
ATOM   1661 O  OD1 . ASN A 1 230 ? -37.585 14.137  -5.292  1.00 33.70 ? 230 ASN A OD1 1 
ATOM   1662 N  ND2 . ASN A 1 230 ? -39.618 13.156  -5.387  1.00 34.87 ? 230 ASN A ND2 1 
ATOM   1663 N  N   . GLU A 1 231 ? -39.387 14.053  -0.976  1.00 33.09 ? 231 GLU A N   1 
ATOM   1664 C  CA  . GLU A 1 231 ? -40.486 14.869  -0.471  1.00 37.55 ? 231 GLU A CA  1 
ATOM   1665 C  C   . GLU A 1 231 ? -40.426 14.847  1.057   1.00 37.42 ? 231 GLU A C   1 
ATOM   1666 O  O   . GLU A 1 231 ? -39.937 13.882  1.619   1.00 34.48 ? 231 GLU A O   1 
ATOM   1667 C  CB  . GLU A 1 231 ? -41.819 14.221  -0.870  1.00 37.79 ? 231 GLU A CB  1 
ATOM   1668 C  CG  . GLU A 1 231 ? -42.165 14.503  -2.326  1.00 50.95 ? 231 GLU A CG  1 
ATOM   1669 C  CD  . GLU A 1 231 ? -43.431 13.801  -2.788  1.00 54.02 ? 231 GLU A CD  1 
ATOM   1670 O  OE1 . GLU A 1 231 ? -44.354 13.714  -1.946  1.00 49.45 ? 231 GLU A OE1 1 
ATOM   1671 O  OE2 . GLU A 1 231 ? -43.489 13.350  -3.957  1.00 61.58 ? 231 GLU A OE2 1 
ATOM   1672 N  N   . ASP A 1 232 ? -40.880 15.921  1.715   1.00 34.25 ? 232 ASP A N   1 
ATOM   1673 C  CA  . ASP A 1 232 ? -41.003 15.939  3.167   1.00 34.26 ? 232 ASP A CA  1 
ATOM   1674 C  C   . ASP A 1 232 ? -42.334 15.348  3.563   1.00 33.97 ? 232 ASP A C   1 
ATOM   1675 O  O   . ASP A 1 232 ? -43.308 15.543  2.851   1.00 35.53 ? 232 ASP A O   1 
ATOM   1676 C  CB  . ASP A 1 232 ? -40.923 17.353  3.714   1.00 38.35 ? 232 ASP A CB  1 
ATOM   1677 C  CG  . ASP A 1 232 ? -39.528 17.926  3.534   1.00 45.55 ? 232 ASP A CG  1 
ATOM   1678 O  OD1 . ASP A 1 232 ? -38.559 17.315  4.061   1.00 45.93 ? 232 ASP A OD1 1 
ATOM   1679 O  OD2 . ASP A 1 232 ? -39.408 18.904  2.792   1.00 54.15 ? 232 ASP A OD2 1 
ATOM   1680 N  N   . PRO A 1 233 ? -42.412 14.625  4.700   1.00 29.73 ? 233 PRO A N   1 
ATOM   1681 C  CA  . PRO A 1 233 ? -41.219 14.301  5.513   1.00 28.06 ? 233 PRO A CA  1 
ATOM   1682 C  C   . PRO A 1 233 ? -40.428 13.196  4.815   1.00 28.02 ? 233 PRO A C   1 
ATOM   1683 O  O   . PRO A 1 233 ? -41.039 12.300  4.204   1.00 29.20 ? 233 PRO A O   1 
ATOM   1684 C  CB  . PRO A 1 233 ? -41.914 13.714  6.791   1.00 29.58 ? 233 PRO A CB  1 
ATOM   1685 C  CG  . PRO A 1 233 ? -43.154 13.010  6.229   1.00 30.53 ? 233 PRO A CG  1 
ATOM   1686 C  CD  . PRO A 1 233 ? -43.671 14.072  5.266   1.00 30.17 ? 233 PRO A CD  1 
ATOM   1687 N  N   . ARG A 1 234 ? -39.137 13.164  5.126   1.00 29.92 ? 234 ARG A N   1 
ATOM   1688 C  CA  A ARG A 1 234 ? -38.358 11.953  4.749   0.50 27.06 ? 234 ARG A CA  1 
ATOM   1689 C  CA  B ARG A 1 234 ? -38.359 11.952  4.748   0.50 27.70 ? 234 ARG A CA  1 
ATOM   1690 C  C   . ARG A 1 234 ? -38.965 10.675  5.454   1.00 28.17 ? 234 ARG A C   1 
ATOM   1691 O  O   . ARG A 1 234 ? -39.576 10.630  6.618   1.00 27.93 ? 234 ARG A O   1 
ATOM   1692 C  CB  A ARG A 1 234 ? -36.932 12.019  5.291   0.50 27.50 ? 234 ARG A CB  1 
ATOM   1693 C  CB  B ARG A 1 234 ? -36.932 12.011  5.286   0.50 29.08 ? 234 ARG A CB  1 
ATOM   1694 C  CG  A ARG A 1 234 ? -35.977 13.042  4.695   0.50 30.23 ? 234 ARG A CG  1 
ATOM   1695 C  CG  B ARG A 1 234 ? -36.035 13.149  4.826   0.50 34.83 ? 234 ARG A CG  1 
ATOM   1696 C  CD  A ARG A 1 234 ? -34.831 13.292  5.660   0.50 29.32 ? 234 ARG A CD  1 
ATOM   1697 C  CD  B ARG A 1 234 ? -34.877 13.297  5.799   0.50 33.68 ? 234 ARG A CD  1 
ATOM   1698 N  NE  A ARG A 1 234 ? -34.217 14.609  5.464   0.50 34.81 ? 234 ARG A NE  1 
ATOM   1699 N  NE  B ARG A 1 234 ? -33.577 13.215  5.128   0.50 32.36 ? 234 ARG A NE  1 
ATOM   1700 C  CZ  A ARG A 1 234 ? -33.103 14.819  4.782   0.50 34.38 ? 234 ARG A CZ  1 
ATOM   1701 C  CZ  B ARG A 1 234 ? -32.921 14.263  4.657   0.50 34.86 ? 234 ARG A CZ  1 
ATOM   1702 N  NH1 A ARG A 1 234 ? -32.450 13.799  4.267   0.50 36.37 ? 234 ARG A NH1 1 
ATOM   1703 N  NH1 B ARG A 1 234 ? -33.399 15.477  4.842   0.50 39.05 ? 234 ARG A NH1 1 
ATOM   1704 N  NH2 A ARG A 1 234 ? -32.647 16.048  4.619   0.50 32.15 ? 234 ARG A NH2 1 
ATOM   1705 N  NH2 B ARG A 1 234 ? -31.789 14.100  4.000   0.50 38.85 ? 234 ARG A NH2 1 
ATOM   1706 N  N   . THR A 1 235 ? -38.993 9.610   4.674   1.00 27.21 ? 235 THR A N   1 
ATOM   1707 C  CA  . THR A 1 235 ? -39.584 8.390   5.205   1.00 28.64 ? 235 THR A CA  1 
ATOM   1708 C  C   . THR A 1 235 ? -38.649 7.197   4.962   1.00 27.61 ? 235 THR A C   1 
ATOM   1709 O  O   . THR A 1 235 ? -37.811 7.227   4.042   1.00 27.44 ? 235 THR A O   1 
ATOM   1710 C  CB  . THR A 1 235 ? -40.991 8.174   4.623   1.00 29.70 ? 235 THR A CB  1 
ATOM   1711 O  OG1 . THR A 1 235 ? -40.955 8.151   3.189   1.00 28.68 ? 235 THR A OG1 1 
ATOM   1712 C  CG2 . THR A 1 235 ? -41.994 9.233   5.066   1.00 28.81 ? 235 THR A CG2 1 
ATOM   1713 N  N   . PHE A 1 236 ? -38.873 6.126   5.745   1.00 25.49 ? 236 PHE A N   1 
ATOM   1714 C  CA  . PHE A 1 236 ? -38.011 4.956   5.694   1.00 23.13 ? 236 PHE A CA  1 
ATOM   1715 C  C   . PHE A 1 236 ? -38.911 3.751   5.516   1.00 25.20 ? 236 PHE A C   1 
ATOM   1716 O  O   . PHE A 1 236 ? -40.054 3.759   5.997   1.00 27.57 ? 236 PHE A O   1 
ATOM   1717 C  CB  . PHE A 1 236 ? -37.211 4.781   7.000   1.00 24.21 ? 236 PHE A CB  1 
ATOM   1718 C  CG  . PHE A 1 236 ? -36.169 5.873   7.267   1.00 25.23 ? 236 PHE A CG  1 
ATOM   1719 C  CD1 . PHE A 1 236 ? -36.539 7.045   7.904   1.00 24.90 ? 236 PHE A CD1 1 
ATOM   1720 C  CD2 . PHE A 1 236 ? -34.828 5.680   6.940   1.00 25.63 ? 236 PHE A CD2 1 
ATOM   1721 C  CE1 . PHE A 1 236 ? -35.587 8.040   8.167   1.00 25.97 ? 236 PHE A CE1 1 
ATOM   1722 C  CE2 . PHE A 1 236 ? -33.851 6.629   7.298   1.00 25.64 ? 236 PHE A CE2 1 
ATOM   1723 C  CZ  . PHE A 1 236 ? -34.252 7.820   7.874   1.00 24.91 ? 236 PHE A CZ  1 
ATOM   1724 N  N   . GLY A 1 237 ? -38.323 2.697   4.958   1.00 23.36 ? 237 GLY A N   1 
ATOM   1725 C  CA  . GLY A 1 237 ? -38.988 1.387   4.944   1.00 24.37 ? 237 GLY A CA  1 
ATOM   1726 C  C   . GLY A 1 237 ? -38.924 0.760   6.345   1.00 26.29 ? 237 GLY A C   1 
ATOM   1727 O  O   . GLY A 1 237 ? -38.356 1.323   7.294   1.00 27.42 ? 237 GLY A O   1 
ATOM   1728 N  N   . GLY A 1 238 ? -39.591 -0.402  6.515   1.00 28.31 ? 238 GLY A N   1 
ATOM   1729 C  CA  . GLY A 1 238 ? -39.763 -0.921  7.868   1.00 26.59 ? 238 GLY A CA  1 
ATOM   1730 C  C   . GLY A 1 238 ? -38.541 -1.751  8.289   1.00 27.87 ? 238 GLY A C   1 
ATOM   1731 O  O   . GLY A 1 238 ? -38.424 -2.159  9.451   1.00 30.56 ? 238 GLY A O   1 
ATOM   1732 N  N   . GLY A 1 239 ? -37.618 -2.006  7.337   1.00 26.85 ? 239 GLY A N   1 
ATOM   1733 C  CA  . GLY A 1 239 ? -36.399 -2.745  7.638   1.00 26.79 ? 239 GLY A CA  1 
ATOM   1734 C  C   . GLY A 1 239 ? -36.472 -4.200  7.170   1.00 29.56 ? 239 GLY A C   1 
ATOM   1735 O  O   . GLY A 1 239 ? -37.542 -4.832  7.188   1.00 29.60 ? 239 GLY A O   1 
ATOM   1736 N  N   . THR A 1 240 ? -35.319 -4.715  6.733   1.00 24.73 ? 240 THR A N   1 
ATOM   1737 C  CA  . THR A 1 240 ? -35.197 -6.126  6.393   1.00 24.95 ? 240 THR A CA  1 
ATOM   1738 C  C   . THR A 1 240 ? -34.021 -6.661  7.200   1.00 24.22 ? 240 THR A C   1 
ATOM   1739 O  O   . THR A 1 240 ? -32.911 -6.200  7.008   1.00 26.35 ? 240 THR A O   1 
ATOM   1740 C  CB  . THR A 1 240 ? -34.891 -6.278  4.902   1.00 24.74 ? 240 THR A CB  1 
ATOM   1741 O  OG1 . THR A 1 240 ? -36.040 -5.803  4.204   1.00 27.94 ? 240 THR A OG1 1 
ATOM   1742 C  CG2 . THR A 1 240 ? -34.649 -7.734  4.565   1.00 27.10 ? 240 THR A CG2 1 
ATOM   1743 N  N   . LYS A 1 241 ? -34.256 -7.708  8.028   1.00 25.45 ? 241 LYS A N   1 
ATOM   1744 C  CA  . LYS A 1 241 ? -33.187 -8.293  8.807   1.00 26.18 ? 241 LYS A CA  1 
ATOM   1745 C  C   . LYS A 1 241 ? -32.605 -9.485  8.052   1.00 28.96 ? 241 LYS A C   1 
ATOM   1746 O  O   . LYS A 1 241 ? -33.294 -10.494 7.828   1.00 30.10 ? 241 LYS A O   1 
ATOM   1747 C  CB  . LYS A 1 241 ? -33.766 -8.695  10.187  1.00 29.73 ? 241 LYS A CB  1 
ATOM   1748 C  CG  . LYS A 1 241 ? -32.697 -9.347  11.041  1.00 36.23 ? 241 LYS A CG  1 
ATOM   1749 C  CD  . LYS A 1 241 ? -33.143 -9.512  12.483  1.00 39.63 ? 241 LYS A CD  1 
ATOM   1750 C  CE  . LYS A 1 241 ? -32.130 -10.357 13.236  1.00 50.92 ? 241 LYS A CE  1 
ATOM   1751 N  NZ  . LYS A 1 241 ? -32.461 -10.320 14.669  1.00 46.37 ? 241 LYS A NZ  1 
ATOM   1752 N  N   . LEU A 1 242 ? -31.324 -9.396  7.729   1.00 27.99 ? 242 LEU A N   1 
ATOM   1753 C  CA  . LEU A 1 242 ? -30.619 -10.467 7.034   1.00 29.03 ? 242 LEU A CA  1 
ATOM   1754 C  C   . LEU A 1 242 ? -29.771 -11.232 8.056   1.00 30.18 ? 242 LEU A C   1 
ATOM   1755 O  O   . LEU A 1 242 ? -28.903 -10.631 8.708   1.00 30.34 ? 242 LEU A O   1 
ATOM   1756 C  CB  . LEU A 1 242 ? -29.715 -9.847  5.961   1.00 27.59 ? 242 LEU A CB  1 
ATOM   1757 C  CG  . LEU A 1 242 ? -28.765 -10.802 5.240   1.00 29.19 ? 242 LEU A CG  1 
ATOM   1758 C  CD1 . LEU A 1 242 ? -29.539 -11.916 4.496   1.00 28.68 ? 242 LEU A CD1 1 
ATOM   1759 C  CD2 . LEU A 1 242 ? -27.788 -10.122 4.265   1.00 30.08 ? 242 LEU A CD2 1 
ATOM   1760 N  N   . GLU A 1 243 ? -29.970 -12.575 8.116   1.00 28.89 ? 243 GLU A N   1 
ATOM   1761 C  CA  . GLU A 1 243 ? -29.082 -13.409 8.918   1.00 31.45 ? 243 GLU A CA  1 
ATOM   1762 C  C   . GLU A 1 243 ? -28.353 -14.419 8.022   1.00 32.54 ? 243 GLU A C   1 
ATOM   1763 O  O   . GLU A 1 243 ? -28.788 -14.684 6.925   1.00 31.95 ? 243 GLU A O   1 
ATOM   1764 C  CB  . GLU A 1 243 ? -29.913 -14.162 9.958   1.00 35.31 ? 243 GLU A CB  1 
ATOM   1765 C  CG  . GLU A 1 243 ? -30.332 -13.242 11.098  0.70 41.82 ? 243 GLU A CG  1 
ATOM   1766 C  CD  . GLU A 1 243 ? -31.276 -13.928 12.064  0.70 46.75 ? 243 GLU A CD  1 
ATOM   1767 O  OE1 . GLU A 1 243 ? -30.757 -14.362 13.108  0.70 51.22 ? 243 GLU A OE1 1 
ATOM   1768 O  OE2 . GLU A 1 243 ? -32.491 -14.001 11.804  0.70 45.44 ? 243 GLU A OE2 1 
ATOM   1769 N  N   . ILE A 1 244 ? -27.255 -15.008 8.529   1.00 32.37 ? 244 ILE A N   1 
ATOM   1770 C  CA  . ILE A 1 244 ? -26.578 -16.067 7.807   1.00 34.27 ? 244 ILE A CA  1 
ATOM   1771 C  C   . ILE A 1 244 ? -27.275 -17.387 8.109   1.00 34.82 ? 244 ILE A C   1 
ATOM   1772 O  O   . ILE A 1 244 ? -27.510 -17.709 9.273   1.00 37.75 ? 244 ILE A O   1 
ATOM   1773 C  CB  . ILE A 1 244 ? -25.107 -16.123 8.233   1.00 38.60 ? 244 ILE A CB  1 
ATOM   1774 C  CG1 . ILE A 1 244 ? -24.391 -14.794 7.861   1.00 39.98 ? 244 ILE A CG1 1 
ATOM   1775 C  CG2 . ILE A 1 244 ? -24.423 -17.330 7.600   1.00 40.14 ? 244 ILE A CG2 1 
ATOM   1776 C  CD1 . ILE A 1 244 ? -24.690 -14.274 6.467   1.00 41.10 ? 244 ILE A CD1 1 
ATOM   1777 N  N   . LYS A 1 245 ? -27.643 -18.135 7.053   1.00 34.43 ? 245 LYS A N   1 
ATOM   1778 C  CA  . LYS A 1 245 ? -28.224 -19.467 7.239   1.00 31.21 ? 245 LYS A CA  1 
ATOM   1779 C  C   . LYS A 1 245 ? -27.062 -20.437 7.387   1.00 39.19 ? 245 LYS A C   1 
ATOM   1780 O  O   . LYS A 1 245 ? -26.335 -20.662 6.422   1.00 42.80 ? 245 LYS A O   1 
ATOM   1781 C  CB  . LYS A 1 245 ? -29.136 -19.850 6.064   1.00 32.15 ? 245 LYS A CB  1 
ATOM   1782 C  CG  . LYS A 1 245 ? -29.939 -21.139 6.177   1.00 35.52 ? 245 LYS A CG  1 
ATOM   1783 C  CD  . LYS A 1 245 ? -31.034 -21.187 5.096   1.00 37.32 ? 245 LYS A CD  1 
ATOM   1784 C  CE  . LYS A 1 245 ? -31.896 -22.454 5.080   1.00 39.29 ? 245 LYS A CE  1 
ATOM   1785 N  NZ  . LYS A 1 245 ? -31.279 -23.590 4.402   1.00 43.26 ? 245 LYS A NZ  1 
ATOM   1786 N  N   . LEU A 1 246 ? -26.915 -20.992 8.605   1.00 41.84 ? 246 LEU A N   1 
ATOM   1787 C  CA  . LEU A 1 246 ? -25.854 -21.920 8.987   1.00 52.18 ? 246 LEU A CA  1 
ATOM   1788 C  C   . LEU A 1 246 ? -26.047 -23.273 8.304   1.00 58.84 ? 246 LEU A C   1 
ATOM   1789 O  O   . LEU A 1 246 ? -27.147 -23.828 8.339   1.00 63.54 ? 246 LEU A O   1 
ATOM   1790 C  CB  . LEU A 1 246 ? -25.965 -22.042 10.506  1.00 53.30 ? 246 LEU A CB  1 
ATOM   1791 C  CG  . LEU A 1 246 ? -25.758 -20.731 11.273  1.00 57.52 ? 246 LEU A CG  1 
ATOM   1792 C  CD1 . LEU A 1 246 ? -25.831 -20.872 12.807  1.00 63.71 ? 246 LEU A CD1 1 
ATOM   1793 C  CD2 . LEU A 1 246 ? -24.437 -20.091 10.824  1.00 56.56 ? 246 LEU A CD2 1 
ATOM   1794 N  N   . GLU A 1 247 ? -24.986 -23.786 7.660   0.70 61.27 ? 247 GLU A N   1 
ATOM   1795 C  CA  . GLU A 1 247 ? -25.099 -25.036 6.914   0.70 61.79 ? 247 GLU A CA  1 
ATOM   1796 C  C   . GLU A 1 247 ? -24.811 -26.222 7.848   0.70 58.34 ? 247 GLU A C   1 
ATOM   1797 O  O   . GLU A 1 247 ? -25.619 -27.175 7.766   0.70 63.57 ? 247 GLU A O   1 
ATOM   1798 C  CB  . GLU A 1 247 ? -24.267 -25.129 5.633   0.70 59.24 ? 247 GLU A CB  1 
HETATM 1799 CL CL  . CL  B 2 .   ? -16.575 -7.680  -1.800  1.00 43.67 ? 301 CL  A CL  1 
HETATM 1800 C  C1  . EDO C 3 .   ? -29.061 13.426  -5.421  1.00 42.00 ? 302 EDO A C1  1 
HETATM 1801 O  O1  . EDO C 3 .   ? -27.654 13.336  -5.138  1.00 36.03 ? 302 EDO A O1  1 
HETATM 1802 C  C2  . EDO C 3 .   ? -29.839 12.266  -4.866  1.00 38.39 ? 302 EDO A C2  1 
HETATM 1803 O  O2  . EDO C 3 .   ? -29.621 12.105  -3.428  1.00 34.14 ? 302 EDO A O2  1 
HETATM 1804 C  C1  . EDO D 3 .   ? -39.762 -7.375  -7.368  1.00 45.31 ? 303 EDO A C1  1 
HETATM 1805 O  O1  . EDO D 3 .   ? -40.605 -6.725  -8.333  1.00 40.95 ? 303 EDO A O1  1 
HETATM 1806 C  C2  . EDO D 3 .   ? -40.207 -7.150  -5.973  1.00 40.68 ? 303 EDO A C2  1 
HETATM 1807 O  O2  . EDO D 3 .   ? -41.574 -7.503  -6.044  1.00 59.67 ? 303 EDO A O2  1 
HETATM 1808 N  N1  . IMD E 4 .   ? -34.294 23.615  10.455  1.00 55.03 ? 304 IMD A N1  1 
HETATM 1809 C  C2  . IMD E 4 .   ? -35.266 24.051  9.615   1.00 51.94 ? 304 IMD A C2  1 
HETATM 1810 N  N3  . IMD E 4 .   ? -35.560 23.056  8.786   1.00 75.48 ? 304 IMD A N3  1 
HETATM 1811 C  C4  . IMD E 4 .   ? -34.785 21.984  9.096   1.00 57.80 ? 304 IMD A C4  1 
HETATM 1812 C  C5  . IMD E 4 .   ? -34.001 22.337  10.143  1.00 53.74 ? 304 IMD A C5  1 
HETATM 1813 C  C1  . EDO F 3 .   ? -45.756 10.288  18.236  1.00 66.58 ? 305 EDO A C1  1 
HETATM 1814 O  O1  . EDO F 3 .   ? -46.834 10.526  19.120  1.00 62.20 ? 305 EDO A O1  1 
HETATM 1815 C  C2  . EDO F 3 .   ? -46.230 9.837   16.905  1.00 65.16 ? 305 EDO A C2  1 
HETATM 1816 O  O2  . EDO F 3 .   ? -46.172 8.436   16.742  1.00 69.97 ? 305 EDO A O2  1 
HETATM 1817 NA NA  . NA  G 5 .   ? -17.908 21.703  18.661  1.00 41.22 ? 306 NA  A NA  1 
HETATM 1818 NA NA  . NA  H 5 .   ? -43.108 -9.276  -1.861  0.80 39.72 ? 307 NA  A NA  1 
HETATM 1819 CL CL  . CL  I 2 .   ? -41.582 -2.405  5.126   0.80 32.96 ? 308 CL  A CL  1 
HETATM 1820 CL CL  . CL  J 2 .   ? -42.507 -9.829  2.151   1.00 39.49 ? 309 CL  A CL  1 
HETATM 1821 CL CL  . CL  K 2 .   ? -42.360 22.522  11.647  1.00 49.13 ? 310 CL  A CL  1 
HETATM 1822 O  O   . HOH L 6 .   ? -42.824 20.521  18.374  1.00 57.74 ? 401 HOH A O   1 
HETATM 1823 O  O   . HOH L 6 .   ? -29.519 27.614  22.123  1.00 48.43 ? 402 HOH A O   1 
HETATM 1824 O  O   . HOH L 6 .   ? -44.411 15.930  29.816  1.00 49.52 ? 403 HOH A O   1 
HETATM 1825 O  O   . HOH L 6 .   ? -42.705 5.131   14.151  1.00 47.68 ? 404 HOH A O   1 
HETATM 1826 O  O   . HOH L 6 .   ? -46.840 0.236   22.736  1.00 40.73 ? 405 HOH A O   1 
HETATM 1827 O  O   . HOH L 6 .   ? -22.807 -20.645 -1.710  1.00 56.25 ? 406 HOH A O   1 
HETATM 1828 O  O   . HOH L 6 .   ? -23.962 -20.425 5.849   1.00 44.19 ? 407 HOH A O   1 
HETATM 1829 O  O   . HOH L 6 .   ? -39.201 -1.551  -11.988 1.00 54.40 ? 408 HOH A O   1 
HETATM 1830 O  O   . HOH L 6 .   ? -20.802 -0.579  11.156  1.00 39.87 ? 409 HOH A O   1 
HETATM 1831 O  O   . HOH L 6 .   ? -29.393 -22.374 2.605   1.00 59.77 ? 410 HOH A O   1 
HETATM 1832 O  O   . HOH L 6 .   ? -31.204 16.052  -8.544  1.00 41.37 ? 411 HOH A O   1 
HETATM 1833 O  O   . HOH L 6 .   ? -36.603 24.751  19.535  1.00 35.97 ? 412 HOH A O   1 
HETATM 1834 O  O   . HOH L 6 .   ? -19.516 9.600   -0.049  1.00 46.44 ? 413 HOH A O   1 
HETATM 1835 O  O   . HOH L 6 .   ? -12.695 16.120  12.584  1.00 51.09 ? 414 HOH A O   1 
HETATM 1836 O  O   . HOH L 6 .   ? -28.788 5.563   31.472  1.00 40.47 ? 415 HOH A O   1 
HETATM 1837 O  O   . HOH L 6 .   ? -40.912 2.992   8.446   1.00 38.83 ? 416 HOH A O   1 
HETATM 1838 O  O   . HOH L 6 .   ? -47.214 21.038  20.360  1.00 53.04 ? 417 HOH A O   1 
HETATM 1839 O  O   . HOH L 6 .   ? -42.335 -7.995  -3.690  1.00 45.67 ? 418 HOH A O   1 
HETATM 1840 O  O   . HOH L 6 .   ? -21.708 -6.342  14.765  1.00 53.94 ? 419 HOH A O   1 
HETATM 1841 O  O   . HOH L 6 .   ? -29.184 1.928   23.579  1.00 33.08 ? 420 HOH A O   1 
HETATM 1842 O  O   . HOH L 6 .   ? -46.380 12.403  8.958   1.00 44.83 ? 421 HOH A O   1 
HETATM 1843 O  O   . HOH L 6 .   ? -48.053 8.170   -1.093  1.00 51.21 ? 422 HOH A O   1 
HETATM 1844 O  O   . HOH L 6 .   ? -38.638 22.757  6.730   1.00 60.26 ? 423 HOH A O   1 
HETATM 1845 O  O   . HOH L 6 .   ? -31.177 11.732  3.308   1.00 40.42 ? 424 HOH A O   1 
HETATM 1846 O  O   . HOH L 6 .   ? -46.225 5.922   14.437  1.00 60.91 ? 425 HOH A O   1 
HETATM 1847 O  O   A HOH L 6 .   ? -26.302 -1.158  -9.920  0.60 42.40 ? 426 HOH A O   1 
HETATM 1848 O  O   B HOH L 6 .   ? -27.596 -0.143  -10.834 0.40 27.66 ? 426 HOH A O   1 
HETATM 1849 O  O   . HOH L 6 .   ? -17.218 13.649  7.555   1.00 55.27 ? 427 HOH A O   1 
HETATM 1850 O  O   . HOH L 6 .   ? -35.450 16.803  6.048   1.00 35.77 ? 428 HOH A O   1 
HETATM 1851 O  O   . HOH L 6 .   ? -30.857 10.383  -1.944  1.00 29.38 ? 429 HOH A O   1 
HETATM 1852 O  O   . HOH L 6 .   ? -40.009 25.104  13.839  1.00 47.82 ? 430 HOH A O   1 
HETATM 1853 O  O   . HOH L 6 .   ? -43.341 9.537   9.154   1.00 34.29 ? 431 HOH A O   1 
HETATM 1854 O  O   A HOH L 6 .   ? -37.871 -3.718  11.512  0.60 26.30 ? 432 HOH A O   1 
HETATM 1855 O  O   B HOH L 6 .   ? -36.755 -4.510  10.723  0.40 26.38 ? 432 HOH A O   1 
HETATM 1856 O  O   . HOH L 6 .   ? -46.168 6.621   18.594  1.00 43.41 ? 433 HOH A O   1 
HETATM 1857 O  O   . HOH L 6 .   ? -44.488 -6.029  -4.481  1.00 48.53 ? 434 HOH A O   1 
HETATM 1858 O  O   . HOH L 6 .   ? -49.212 0.613   28.155  1.00 60.37 ? 435 HOH A O   1 
HETATM 1859 O  O   . HOH L 6 .   ? -46.235 8.409   20.982  1.00 39.67 ? 436 HOH A O   1 
HETATM 1860 O  O   . HOH L 6 .   ? -46.773 14.485  3.137   1.00 44.00 ? 437 HOH A O   1 
HETATM 1861 O  O   . HOH L 6 .   ? -28.204 13.210  28.562  1.00 45.19 ? 438 HOH A O   1 
HETATM 1862 O  O   . HOH L 6 .   ? -43.826 18.564  23.739  1.00 48.86 ? 439 HOH A O   1 
HETATM 1863 O  O   . HOH L 6 .   ? -26.458 1.693   17.667  1.00 32.36 ? 440 HOH A O   1 
HETATM 1864 O  O   A HOH L 6 .   ? -33.527 15.498  -16.446 0.50 36.49 ? 441 HOH A O   1 
HETATM 1865 O  O   B HOH L 6 .   ? -33.909 13.423  -16.796 0.50 40.31 ? 441 HOH A O   1 
HETATM 1866 O  O   . HOH L 6 .   ? -33.980 -5.595  12.800  1.00 42.13 ? 442 HOH A O   1 
HETATM 1867 O  O   . HOH L 6 .   ? -28.473 27.988  18.371  1.00 48.47 ? 443 HOH A O   1 
HETATM 1868 O  O   . HOH L 6 .   ? -43.651 1.182   5.389   1.00 54.26 ? 444 HOH A O   1 
HETATM 1869 O  O   . HOH L 6 .   ? -35.958 28.225  8.809   1.00 53.11 ? 445 HOH A O   1 
HETATM 1870 O  O   . HOH L 6 .   ? -21.757 6.958   12.996  1.00 42.83 ? 446 HOH A O   1 
HETATM 1871 O  O   . HOH L 6 .   ? -14.425 13.963  18.114  1.00 58.47 ? 447 HOH A O   1 
HETATM 1872 O  O   . HOH L 6 .   ? -20.934 24.506  19.216  1.00 53.46 ? 448 HOH A O   1 
HETATM 1873 O  O   . HOH L 6 .   ? -40.727 9.338   8.609   1.00 27.28 ? 449 HOH A O   1 
HETATM 1874 O  O   . HOH L 6 .   ? -44.284 -0.417  -7.562  1.00 48.70 ? 450 HOH A O   1 
HETATM 1875 O  O   . HOH L 6 .   ? -36.668 -1.664  12.816  1.00 32.56 ? 451 HOH A O   1 
HETATM 1876 O  O   . HOH L 6 .   ? -25.771 5.296   22.638  1.00 34.75 ? 452 HOH A O   1 
HETATM 1877 O  O   . HOH L 6 .   ? -23.970 0.999   18.577  1.00 36.70 ? 453 HOH A O   1 
HETATM 1878 O  O   . HOH L 6 .   ? -29.915 13.841  -1.455  1.00 35.00 ? 454 HOH A O   1 
HETATM 1879 O  O   . HOH L 6 .   ? -39.022 24.006  18.183  1.00 38.03 ? 455 HOH A O   1 
HETATM 1880 O  O   . HOH L 6 .   ? -44.842 0.579   28.818  1.00 37.28 ? 456 HOH A O   1 
HETATM 1881 O  O   . HOH L 6 .   ? -21.647 -11.133 -7.803  1.00 48.40 ? 457 HOH A O   1 
HETATM 1882 O  O   . HOH L 6 .   ? -27.169 9.491   4.842   1.00 27.75 ? 458 HOH A O   1 
HETATM 1883 O  O   . HOH L 6 .   ? -37.852 11.263  32.878  1.00 48.97 ? 459 HOH A O   1 
HETATM 1884 O  O   . HOH L 6 .   ? -14.623 2.991   -1.221  1.00 56.02 ? 460 HOH A O   1 
HETATM 1885 O  O   . HOH L 6 .   ? -45.237 8.897   7.374   1.00 41.98 ? 461 HOH A O   1 
HETATM 1886 O  O   . HOH L 6 .   ? -24.700 5.190   -10.115 1.00 57.93 ? 462 HOH A O   1 
HETATM 1887 O  O   . HOH L 6 .   ? -31.336 -2.713  13.535  1.00 35.61 ? 463 HOH A O   1 
HETATM 1888 O  O   . HOH L 6 .   ? -22.653 5.329   11.215  1.00 36.32 ? 464 HOH A O   1 
HETATM 1889 O  O   . HOH L 6 .   ? -21.057 4.111   5.568   1.00 27.36 ? 465 HOH A O   1 
HETATM 1890 O  O   . HOH L 6 .   ? -45.075 1.292   -0.409  1.00 33.83 ? 466 HOH A O   1 
HETATM 1891 O  O   . HOH L 6 .   ? -21.111 5.532   -8.312  1.00 49.06 ? 467 HOH A O   1 
HETATM 1892 O  O   . HOH L 6 .   ? -43.432 1.676   21.760  1.00 33.07 ? 468 HOH A O   1 
HETATM 1893 O  O   . HOH L 6 .   ? -43.141 2.925   36.648  1.00 42.43 ? 469 HOH A O   1 
HETATM 1894 O  O   . HOH L 6 .   ? -37.750 0.973   -11.529 1.00 54.50 ? 470 HOH A O   1 
HETATM 1895 O  O   . HOH L 6 .   ? -20.904 10.390  3.120   1.00 33.05 ? 471 HOH A O   1 
HETATM 1896 O  O   . HOH L 6 .   ? -46.703 14.609  6.957   1.00 51.74 ? 472 HOH A O   1 
HETATM 1897 O  O   . HOH L 6 .   ? -34.436 26.332  18.806  1.00 43.94 ? 473 HOH A O   1 
HETATM 1898 O  O   . HOH L 6 .   ? -22.764 6.678   24.835  1.00 52.69 ? 474 HOH A O   1 
HETATM 1899 O  O   . HOH L 6 .   ? -33.688 -12.584 9.830   1.00 39.31 ? 475 HOH A O   1 
HETATM 1900 O  O   . HOH L 6 .   ? -18.869 13.874  20.564  1.00 38.09 ? 476 HOH A O   1 
HETATM 1901 O  O   . HOH L 6 .   ? -28.073 2.015   20.980  1.00 39.55 ? 477 HOH A O   1 
HETATM 1902 O  O   . HOH L 6 .   ? -26.820 15.781  -4.302  1.00 46.16 ? 478 HOH A O   1 
HETATM 1903 O  O   . HOH L 6 .   ? -23.178 18.170  26.527  1.00 46.17 ? 479 HOH A O   1 
HETATM 1904 O  O   . HOH L 6 .   ? -32.761 -1.080  22.781  1.00 32.86 ? 480 HOH A O   1 
HETATM 1905 O  O   A HOH L 6 .   ? -38.988 24.976  9.438   0.50 29.76 ? 481 HOH A O   1 
HETATM 1906 O  O   B HOH L 6 .   ? -40.764 24.549  9.596   0.50 33.69 ? 481 HOH A O   1 
HETATM 1907 O  O   . HOH L 6 .   ? -32.236 5.815   -10.525 1.00 41.38 ? 482 HOH A O   1 
HETATM 1908 O  O   . HOH L 6 .   ? -29.845 10.909  22.721  1.00 27.18 ? 483 HOH A O   1 
HETATM 1909 O  O   . HOH L 6 .   ? -37.927 15.537  6.028   1.00 32.92 ? 484 HOH A O   1 
HETATM 1910 O  O   A HOH L 6 .   ? -48.172 12.767  19.919  0.60 35.05 ? 485 HOH A O   1 
HETATM 1911 O  O   B HOH L 6 .   ? -48.199 14.176  21.366  0.40 30.36 ? 485 HOH A O   1 
HETATM 1912 O  O   . HOH L 6 .   ? -23.467 7.840   20.090  1.00 29.94 ? 486 HOH A O   1 
HETATM 1913 O  O   A HOH L 6 .   ? -25.008 -8.369  -7.720  0.50 31.33 ? 487 HOH A O   1 
HETATM 1914 O  O   B HOH L 6 .   ? -23.694 -9.505  -8.660  0.50 36.14 ? 487 HOH A O   1 
HETATM 1915 O  O   A HOH L 6 .   ? -22.711 -13.099 10.945  0.50 38.83 ? 488 HOH A O   1 
HETATM 1916 O  O   . HOH L 6 .   ? -42.228 8.732   20.183  1.00 31.03 ? 489 HOH A O   1 
HETATM 1917 O  O   . HOH L 6 .   ? -43.589 11.938  -6.493  1.00 58.05 ? 490 HOH A O   1 
HETATM 1918 O  O   . HOH L 6 .   ? -21.180 6.855   5.778   1.00 32.81 ? 491 HOH A O   1 
HETATM 1919 O  O   . HOH L 6 .   ? -41.092 -10.980 4.578   1.00 39.08 ? 492 HOH A O   1 
HETATM 1920 O  O   . HOH L 6 .   ? -33.872 2.276   28.551  1.00 31.16 ? 493 HOH A O   1 
HETATM 1921 O  O   . HOH L 6 .   ? -38.468 -3.273  -6.108  1.00 30.00 ? 494 HOH A O   1 
HETATM 1922 O  O   . HOH L 6 .   ? -19.466 -9.448  -6.025  1.00 49.05 ? 495 HOH A O   1 
HETATM 1923 O  O   . HOH L 6 .   ? -32.146 -19.150 2.020   1.00 55.91 ? 496 HOH A O   1 
HETATM 1924 O  O   . HOH L 6 .   ? -24.499 20.036  13.777  1.00 27.89 ? 497 HOH A O   1 
HETATM 1925 O  O   . HOH L 6 .   ? -29.900 8.169   -8.900  1.00 34.24 ? 498 HOH A O   1 
HETATM 1926 O  O   . HOH L 6 .   ? -40.639 9.197   -12.028 1.00 52.49 ? 499 HOH A O   1 
HETATM 1927 O  O   . HOH L 6 .   ? -48.463 8.181   22.588  1.00 48.39 ? 500 HOH A O   1 
HETATM 1928 O  O   . HOH L 6 .   ? -18.477 3.322   4.871   1.00 37.70 ? 501 HOH A O   1 
HETATM 1929 O  O   . HOH L 6 .   ? -22.563 -8.071  10.770  1.00 38.52 ? 502 HOH A O   1 
HETATM 1930 O  O   . HOH L 6 .   ? -26.820 13.345  -11.505 1.00 56.24 ? 503 HOH A O   1 
HETATM 1931 O  O   . HOH L 6 .   ? -31.742 -1.084  17.835  1.00 34.82 ? 504 HOH A O   1 
HETATM 1932 O  O   . HOH L 6 .   ? -47.904 0.587   37.067  1.00 50.37 ? 505 HOH A O   1 
HETATM 1933 O  O   . HOH L 6 .   ? -25.017 12.891  25.069  1.00 44.36 ? 506 HOH A O   1 
HETATM 1934 O  O   . HOH L 6 .   ? -39.089 -4.431  -8.653  1.00 39.85 ? 507 HOH A O   1 
HETATM 1935 O  O   . HOH L 6 .   ? -31.878 23.015  7.973   1.00 57.28 ? 508 HOH A O   1 
HETATM 1936 O  O   . HOH L 6 .   ? -45.138 13.426  1.078   1.00 50.10 ? 509 HOH A O   1 
HETATM 1937 O  O   . HOH L 6 .   ? -43.001 -0.000  26.751  0.50 36.99 ? 510 HOH A O   1 
HETATM 1938 O  O   . HOH L 6 .   ? -18.863 -15.721 1.621   1.00 50.55 ? 511 HOH A O   1 
HETATM 1939 O  O   . HOH L 6 .   ? -21.356 -5.515  5.423   1.00 31.61 ? 512 HOH A O   1 
HETATM 1940 O  O   . HOH L 6 .   ? -15.412 -6.732  2.950   1.00 51.47 ? 513 HOH A O   1 
HETATM 1941 O  O   . HOH L 6 .   ? -30.319 11.817  27.910  1.00 46.89 ? 514 HOH A O   1 
HETATM 1942 O  O   . HOH L 6 .   ? -43.356 -6.834  2.347   1.00 47.16 ? 515 HOH A O   1 
HETATM 1943 O  O   . HOH L 6 .   ? -26.158 17.693  8.180   1.00 28.09 ? 516 HOH A O   1 
HETATM 1944 O  O   . HOH L 6 .   ? -31.598 0.785   -5.064  1.00 26.52 ? 517 HOH A O   1 
HETATM 1945 O  O   . HOH L 6 .   ? -32.189 -12.558 -6.850  1.00 39.90 ? 518 HOH A O   1 
HETATM 1946 O  O   . HOH L 6 .   ? -24.879 29.654  9.356   1.00 44.79 ? 519 HOH A O   1 
HETATM 1947 O  O   A HOH L 6 .   ? -27.261 -2.308  16.422  0.50 35.18 ? 520 HOH A O   1 
HETATM 1948 O  O   B HOH L 6 .   ? -27.265 -0.948  17.725  0.50 27.11 ? 520 HOH A O   1 
HETATM 1949 O  O   . HOH L 6 .   ? -18.934 19.918  17.318  1.00 33.25 ? 521 HOH A O   1 
HETATM 1950 O  O   . HOH L 6 .   ? -17.897 7.895   4.063   1.00 53.04 ? 522 HOH A O   1 
HETATM 1951 O  O   . HOH L 6 .   ? -28.769 -4.745  13.577  1.00 39.30 ? 523 HOH A O   1 
HETATM 1952 O  O   . HOH L 6 .   ? -23.374 -17.911 -5.457  1.00 51.84 ? 524 HOH A O   1 
HETATM 1953 O  O   . HOH L 6 .   ? -22.024 7.110   9.278   1.00 38.91 ? 525 HOH A O   1 
HETATM 1954 O  O   . HOH L 6 .   ? -33.524 -12.544 -1.435  1.00 31.58 ? 526 HOH A O   1 
HETATM 1955 O  O   . HOH L 6 .   ? -40.275 -4.279  7.003   1.00 45.37 ? 527 HOH A O   1 
HETATM 1956 O  O   . HOH L 6 .   ? -48.595 11.009  23.679  1.00 45.79 ? 528 HOH A O   1 
HETATM 1957 O  O   . HOH L 6 .   ? -26.879 2.452   29.220  1.00 56.59 ? 529 HOH A O   1 
HETATM 1958 O  O   . HOH L 6 .   ? -14.788 -3.955  -2.513  1.00 50.22 ? 530 HOH A O   1 
HETATM 1959 O  O   . HOH L 6 .   ? -24.869 -0.326  -7.424  1.00 34.75 ? 531 HOH A O   1 
HETATM 1960 O  O   . HOH L 6 .   ? -40.575 3.615   14.340  1.00 32.10 ? 532 HOH A O   1 
HETATM 1961 O  O   . HOH L 6 .   ? -43.248 11.827  2.355   1.00 32.29 ? 533 HOH A O   1 
HETATM 1962 O  O   . HOH L 6 .   ? -30.121 18.129  6.062   1.00 31.37 ? 534 HOH A O   1 
HETATM 1963 O  O   . HOH L 6 .   ? -40.676 6.632   7.827   1.00 28.78 ? 535 HOH A O   1 
HETATM 1964 O  O   . HOH L 6 .   ? -42.596 4.092   4.867   1.00 34.96 ? 536 HOH A O   1 
HETATM 1965 O  O   . HOH L 6 .   ? -19.888 10.587  5.817   1.00 35.75 ? 537 HOH A O   1 
HETATM 1966 O  O   A HOH L 6 .   ? -30.413 2.864   -10.459 0.60 34.79 ? 538 HOH A O   1 
HETATM 1967 O  O   B HOH L 6 .   ? -29.307 1.683   -11.818 0.40 36.74 ? 538 HOH A O   1 
HETATM 1968 O  O   . HOH L 6 .   ? -24.433 -7.188  -5.632  1.00 48.03 ? 539 HOH A O   1 
HETATM 1969 O  O   . HOH L 6 .   ? -26.548 11.727  -7.164  1.00 39.30 ? 540 HOH A O   1 
HETATM 1970 O  O   . HOH L 6 .   ? -24.560 -14.245 -9.049  1.00 51.42 ? 541 HOH A O   1 
HETATM 1971 O  O   . HOH L 6 .   ? -22.209 28.507  11.349  1.00 51.36 ? 542 HOH A O   1 
HETATM 1972 O  O   . HOH L 6 .   ? -18.414 8.697   14.702  1.00 46.03 ? 543 HOH A O   1 
HETATM 1973 O  O   . HOH L 6 .   ? -45.485 -0.456  3.977   1.00 55.76 ? 544 HOH A O   1 
HETATM 1974 O  O   . HOH L 6 .   ? -18.376 22.997  22.675  1.00 44.78 ? 545 HOH A O   1 
HETATM 1975 O  O   . HOH L 6 .   ? -29.771 -4.526  -7.143  1.00 31.91 ? 546 HOH A O   1 
HETATM 1976 O  O   . HOH L 6 .   ? -32.356 5.474   33.241  1.00 39.68 ? 547 HOH A O   1 
HETATM 1977 O  O   . HOH L 6 .   ? -29.319 5.246   -10.489 1.00 46.97 ? 548 HOH A O   1 
HETATM 1978 O  O   . HOH L 6 .   ? -17.730 3.752   -3.017  1.00 53.50 ? 549 HOH A O   1 
HETATM 1979 O  O   . HOH L 6 .   ? -20.156 6.138   -5.376  1.00 51.26 ? 550 HOH A O   1 
HETATM 1980 O  O   . HOH L 6 .   ? -44.631 6.845   5.221   1.00 50.93 ? 551 HOH A O   1 
HETATM 1981 O  O   . HOH L 6 .   ? -32.035 18.871  18.698  1.00 27.80 ? 552 HOH A O   1 
HETATM 1982 O  O   . HOH L 6 .   ? -29.479 12.605  -13.534 1.00 54.92 ? 553 HOH A O   1 
HETATM 1983 O  O   . HOH L 6 .   ? -30.347 21.122  5.811   1.00 34.04 ? 554 HOH A O   1 
HETATM 1984 O  O   . HOH L 6 .   ? -35.212 16.820  -1.854  1.00 39.09 ? 555 HOH A O   1 
HETATM 1985 O  O   . HOH L 6 .   ? -41.042 -4.306  -1.793  1.00 31.38 ? 556 HOH A O   1 
HETATM 1986 O  O   . HOH L 6 .   ? -35.050 20.102  23.569  1.00 36.82 ? 557 HOH A O   1 
HETATM 1987 O  O   . HOH L 6 .   ? -44.006 6.512   16.078  1.00 32.92 ? 558 HOH A O   1 
HETATM 1988 O  O   . HOH L 6 .   ? -28.866 -9.856  11.474  1.00 36.31 ? 559 HOH A O   1 
HETATM 1989 O  O   . HOH L 6 .   ? -17.094 1.781   -2.133  1.00 41.41 ? 560 HOH A O   1 
HETATM 1990 O  O   . HOH L 6 .   ? -28.077 16.234  6.920   1.00 32.10 ? 561 HOH A O   1 
HETATM 1991 O  O   . HOH L 6 .   ? -41.728 17.876  23.705  1.00 32.96 ? 562 HOH A O   1 
HETATM 1992 O  O   . HOH L 6 .   ? -40.307 2.028   -11.328 1.00 51.27 ? 563 HOH A O   1 
HETATM 1993 O  O   . HOH L 6 .   ? -42.870 21.631  24.108  1.00 67.70 ? 564 HOH A O   1 
HETATM 1994 O  O   . HOH L 6 .   ? -20.967 9.194   15.868  1.00 41.60 ? 565 HOH A O   1 
HETATM 1995 O  O   . HOH L 6 .   ? -43.761 -0.199  -10.857 1.00 59.05 ? 566 HOH A O   1 
HETATM 1996 O  O   . HOH L 6 .   ? -47.013 14.781  18.206  1.00 44.52 ? 567 HOH A O   1 
HETATM 1997 O  O   . HOH L 6 .   ? -48.966 8.451   29.780  1.00 57.40 ? 568 HOH A O   1 
HETATM 1998 O  O   . HOH L 6 .   ? -16.716 21.748  10.189  1.00 36.23 ? 569 HOH A O   1 
HETATM 1999 O  O   . HOH L 6 .   ? -45.050 16.252  8.189   1.00 35.14 ? 570 HOH A O   1 
HETATM 2000 O  O   . HOH L 6 .   ? -23.793 -0.674  10.810  1.00 31.81 ? 571 HOH A O   1 
HETATM 2001 O  O   . HOH L 6 .   ? -21.340 10.635  -6.673  1.00 44.49 ? 572 HOH A O   1 
HETATM 2002 O  O   . HOH L 6 .   ? -23.639 -1.706  21.204  1.00 58.75 ? 573 HOH A O   1 
HETATM 2003 O  O   . HOH L 6 .   ? -49.054 13.082  30.380  1.00 58.16 ? 574 HOH A O   1 
HETATM 2004 O  O   . HOH L 6 .   ? -19.692 8.808   9.102   1.00 53.00 ? 575 HOH A O   1 
HETATM 2005 O  O   . HOH L 6 .   ? -34.775 29.818  15.541  1.00 56.35 ? 576 HOH A O   1 
HETATM 2006 O  O   . HOH L 6 .   ? -22.236 -1.823  -6.962  1.00 46.71 ? 577 HOH A O   1 
HETATM 2007 O  O   . HOH L 6 .   ? -31.108 18.417  -10.170 1.00 46.19 ? 578 HOH A O   1 
HETATM 2008 O  O   . HOH L 6 .   ? -37.949 27.287  13.177  1.00 41.55 ? 579 HOH A O   1 
HETATM 2009 O  O   . HOH L 6 .   ? -35.015 -16.867 4.435   1.00 32.74 ? 580 HOH A O   1 
HETATM 2010 O  O   . HOH L 6 .   ? -43.917 -0.184  37.747  1.00 41.23 ? 581 HOH A O   1 
HETATM 2011 O  O   . HOH L 6 .   ? -26.361 -15.357 -7.770  1.00 32.63 ? 582 HOH A O   1 
HETATM 2012 O  O   . HOH L 6 .   ? -14.458 19.041  18.489  1.00 36.96 ? 583 HOH A O   1 
HETATM 2013 O  O   . HOH L 6 .   ? -26.369 -14.156 11.194  1.00 31.99 ? 584 HOH A O   1 
HETATM 2014 O  O   . HOH L 6 .   ? -37.396 -6.779  10.074  1.00 51.92 ? 585 HOH A O   1 
HETATM 2015 O  O   A HOH L 6 .   ? -26.808 8.409   -9.489  0.50 31.90 ? 586 HOH A O   1 
HETATM 2016 O  O   B HOH L 6 .   ? -27.757 10.097  -9.239  0.50 32.32 ? 586 HOH A O   1 
HETATM 2017 O  O   . HOH L 6 .   ? -19.950 -17.635 -3.961  1.00 57.51 ? 587 HOH A O   1 
HETATM 2018 O  O   . HOH L 6 .   ? -30.551 18.726  2.272   1.00 52.94 ? 588 HOH A O   1 
HETATM 2019 O  O   . HOH L 6 .   ? -27.731 -4.234  -8.874  1.00 49.82 ? 589 HOH A O   1 
HETATM 2020 O  O   . HOH L 6 .   ? -34.358 13.953  31.324  1.00 40.51 ? 590 HOH A O   1 
HETATM 2021 O  O   . HOH L 6 .   ? -43.280 -9.920  -6.125  1.00 40.37 ? 591 HOH A O   1 
HETATM 2022 O  O   . HOH L 6 .   ? -29.204 -19.238 0.737   1.00 36.53 ? 592 HOH A O   1 
HETATM 2023 O  O   . HOH L 6 .   ? -27.135 27.948  21.170  1.00 45.32 ? 593 HOH A O   1 
HETATM 2024 O  O   . HOH L 6 .   ? -18.475 -4.266  5.416   1.00 36.23 ? 594 HOH A O   1 
HETATM 2025 O  O   . HOH L 6 .   ? -24.969 28.552  23.579  1.00 50.24 ? 595 HOH A O   1 
HETATM 2026 O  O   . HOH L 6 .   ? -37.989 15.908  -12.601 1.00 44.27 ? 596 HOH A O   1 
HETATM 2027 O  O   . HOH L 6 .   ? -45.581 10.933  35.498  1.00 54.87 ? 597 HOH A O   1 
HETATM 2028 O  O   . HOH L 6 .   ? -20.721 -7.446  12.300  1.00 49.20 ? 598 HOH A O   1 
HETATM 2029 O  O   . HOH L 6 .   ? -43.262 -1.939  8.469   1.00 55.00 ? 599 HOH A O   1 
HETATM 2030 O  O   . HOH L 6 .   ? -19.031 8.982   -2.540  1.00 51.73 ? 600 HOH A O   1 
HETATM 2031 O  O   . HOH L 6 .   ? -32.473 20.737  -10.910 1.00 48.45 ? 601 HOH A O   1 
HETATM 2032 O  O   . HOH L 6 .   ? -28.915 15.634  -12.164 1.00 42.42 ? 602 HOH A O   1 
HETATM 2033 O  O   . HOH L 6 .   ? -16.269 9.864   11.787  1.00 54.09 ? 603 HOH A O   1 
HETATM 2034 O  O   . HOH L 6 .   ? -45.685 9.149   -8.564  1.00 47.76 ? 604 HOH A O   1 
HETATM 2035 O  O   . HOH L 6 .   ? -17.381 -1.472  5.275   1.00 39.71 ? 605 HOH A O   1 
HETATM 2036 O  O   . HOH L 6 .   ? -22.545 -16.284 10.934  1.00 60.70 ? 606 HOH A O   1 
HETATM 2037 O  O   . HOH L 6 .   ? -18.746 -1.693  9.765   1.00 38.17 ? 607 HOH A O   1 
HETATM 2038 O  O   . HOH L 6 .   ? -29.763 -19.641 -2.576  1.00 61.72 ? 608 HOH A O   1 
HETATM 2039 O  O   . HOH L 6 .   ? -20.840 2.859   -7.017  1.00 33.04 ? 609 HOH A O   1 
HETATM 2040 O  O   . HOH L 6 .   ? -16.863 24.669  9.249   1.00 21.33 ? 610 HOH A O   1 
HETATM 2041 O  O   . HOH L 6 .   ? -17.359 19.993  20.290  1.00 48.45 ? 611 HOH A O   1 
HETATM 2042 O  O   . HOH L 6 .   ? -40.814 14.662  33.936  1.00 41.46 ? 612 HOH A O   1 
HETATM 2043 O  O   . HOH L 6 .   ? -49.926 4.949   -4.088  1.00 54.30 ? 613 HOH A O   1 
HETATM 2044 O  O   . HOH L 6 .   ? -13.803 11.844  11.058  1.00 58.18 ? 614 HOH A O   1 
HETATM 2045 O  O   . HOH L 6 .   ? -29.466 12.067  0.984   1.00 32.35 ? 615 HOH A O   1 
HETATM 2046 O  O   . HOH L 6 .   ? -17.247 -11.559 7.003   1.00 44.03 ? 616 HOH A O   1 
HETATM 2047 O  O   . HOH L 6 .   ? -18.675 2.618   8.608   1.00 51.27 ? 617 HOH A O   1 
HETATM 2048 O  O   . HOH L 6 .   ? -30.158 15.622  28.472  1.00 53.41 ? 618 HOH A O   1 
HETATM 2049 O  O   . HOH L 6 .   ? -32.058 0.363   -12.680 1.00 39.85 ? 619 HOH A O   1 
HETATM 2050 O  O   . HOH L 6 .   ? -27.231 5.241   29.778  1.00 50.13 ? 620 HOH A O   1 
HETATM 2051 O  O   . HOH L 6 .   ? -48.537 4.387   28.660  1.00 37.86 ? 621 HOH A O   1 
HETATM 2052 O  O   . HOH L 6 .   ? -17.734 -14.833 5.851   1.00 42.33 ? 622 HOH A O   1 
HETATM 2053 O  O   . HOH L 6 .   ? -32.400 25.925  20.374  1.00 32.11 ? 623 HOH A O   1 
HETATM 2054 O  O   . HOH L 6 .   ? -49.394 10.478  5.455   1.00 52.93 ? 624 HOH A O   1 
HETATM 2055 O  O   . HOH L 6 .   ? -37.253 27.387  16.389  1.00 56.42 ? 625 HOH A O   1 
HETATM 2056 O  O   . HOH L 6 .   ? -36.980 12.230  -13.115 1.00 36.33 ? 626 HOH A O   1 
HETATM 2057 O  O   . HOH L 6 .   ? -23.152 3.068   -9.873  1.00 61.78 ? 627 HOH A O   1 
HETATM 2058 O  O   . HOH L 6 .   ? -18.604 11.837  3.096   1.00 45.33 ? 628 HOH A O   1 
HETATM 2059 O  O   . HOH L 6 .   ? -18.292 23.463  17.011  1.00 39.62 ? 629 HOH A O   1 
HETATM 2060 O  O   . HOH L 6 .   ? -28.306 -17.471 -4.072  1.00 46.13 ? 630 HOH A O   1 
HETATM 2061 O  O   . HOH L 6 .   ? -41.869 18.207  -0.137  1.00 41.15 ? 631 HOH A O   1 
HETATM 2062 O  O   . HOH L 6 .   ? -24.428 6.142   28.614  1.00 39.22 ? 632 HOH A O   1 
HETATM 2063 O  O   . HOH L 6 .   ? -20.338 25.768  16.556  1.00 35.50 ? 633 HOH A O   1 
HETATM 2064 O  O   . HOH L 6 .   ? -46.818 7.609   9.926   1.00 61.69 ? 634 HOH A O   1 
HETATM 2065 O  O   . HOH L 6 .   ? -29.324 16.965  -1.561  1.00 46.62 ? 635 HOH A O   1 
HETATM 2066 O  O   . HOH L 6 .   ? -16.425 1.487   5.521   1.00 56.62 ? 636 HOH A O   1 
HETATM 2067 O  O   . HOH L 6 .   ? -28.374 -4.946  17.717  1.00 58.59 ? 637 HOH A O   1 
HETATM 2068 O  O   . HOH L 6 .   ? -29.681 -7.202  12.598  1.00 30.28 ? 638 HOH A O   1 
HETATM 2069 O  O   . HOH L 6 .   ? -15.925 21.356  17.335  1.00 50.93 ? 639 HOH A O   1 
HETATM 2070 O  O   . HOH L 6 .   ? -48.033 2.294   30.601  1.00 53.00 ? 640 HOH A O   1 
HETATM 2071 O  O   . HOH L 6 .   ? -40.031 -12.612 5.971   1.00 45.99 ? 641 HOH A O   1 
HETATM 2072 O  O   . HOH L 6 .   ? -39.205 9.341   34.582  1.00 32.70 ? 642 HOH A O   1 
HETATM 2073 O  O   . HOH L 6 .   ? -37.417 17.030  30.029  1.00 40.98 ? 643 HOH A O   1 
HETATM 2074 O  O   . HOH L 6 .   ? -14.036 -9.056  2.524   1.00 66.21 ? 644 HOH A O   1 
HETATM 2075 O  O   . HOH L 6 .   ? -30.538 27.790  19.961  1.00 49.74 ? 645 HOH A O   1 
HETATM 2076 O  O   . HOH L 6 .   ? -44.152 -7.326  -0.870  1.00 52.75 ? 646 HOH A O   1 
HETATM 2077 O  O   . HOH L 6 .   ? -47.101 15.231  23.696  1.00 41.89 ? 647 HOH A O   1 
HETATM 2078 O  O   . HOH L 6 .   ? -49.877 11.291  26.610  1.00 50.28 ? 648 HOH A O   1 
HETATM 2079 O  O   . HOH L 6 .   ? -42.591 0.909   7.968   1.00 47.38 ? 649 HOH A O   1 
HETATM 2080 O  O   . HOH L 6 .   ? -45.543 19.760  11.659  1.00 51.76 ? 650 HOH A O   1 
HETATM 2081 O  O   . HOH L 6 .   ? -39.528 15.659  -7.584  1.00 61.50 ? 651 HOH A O   1 
HETATM 2082 O  O   . HOH L 6 .   ? -32.404 30.248  18.951  1.00 64.63 ? 652 HOH A O   1 
HETATM 2083 O  O   . HOH L 6 .   ? -21.601 2.708   11.740  1.00 45.23 ? 653 HOH A O   1 
HETATM 2084 O  O   . HOH L 6 .   ? -17.009 -2.690  17.213  1.00 75.01 ? 654 HOH A O   1 
HETATM 2085 O  O   . HOH L 6 .   ? -34.560 -15.066 9.368   1.00 50.35 ? 655 HOH A O   1 
HETATM 2086 O  O   . HOH L 6 .   ? -16.972 10.680  0.638   1.00 57.91 ? 656 HOH A O   1 
HETATM 2087 O  O   . HOH L 6 .   ? -23.457 10.374  26.527  1.00 52.06 ? 657 HOH A O   1 
HETATM 2088 O  O   . HOH L 6 .   ? -40.876 16.566  -4.895  1.00 60.43 ? 658 HOH A O   1 
HETATM 2089 O  O   A HOH L 6 .   ? -30.533 23.858  24.837  0.70 39.81 ? 659 HOH A O   1 
HETATM 2090 O  O   B HOH L 6 .   ? -31.990 22.950  25.490  0.30 28.49 ? 659 HOH A O   1 
HETATM 2091 O  O   A HOH L 6 .   ? -13.732 20.840  14.627  0.50 33.63 ? 660 HOH A O   1 
HETATM 2092 O  O   B HOH L 6 .   ? -12.692 19.577  15.321  0.50 40.30 ? 660 HOH A O   1 
HETATM 2093 O  O   . HOH L 6 .   ? -16.305 23.051  19.900  1.00 50.49 ? 661 HOH A O   1 
HETATM 2094 O  O   . HOH L 6 .   ? -36.479 -15.654 7.805   1.00 48.40 ? 662 HOH A O   1 
HETATM 2095 O  O   . HOH L 6 .   ? -45.946 19.561  24.662  1.00 64.74 ? 663 HOH A O   1 
HETATM 2096 O  O   . HOH L 6 .   ? -26.551 -30.522 7.402   1.00 72.64 ? 664 HOH A O   1 
HETATM 2097 O  O   . HOH L 6 .   ? -18.667 -18.692 0.952   1.00 55.39 ? 665 HOH A O   1 
HETATM 2098 O  O   . HOH L 6 .   ? -42.628 17.290  7.067   1.00 33.76 ? 666 HOH A O   1 
HETATM 2099 O  O   . HOH L 6 .   ? -19.424 12.267  0.230   1.00 38.52 ? 667 HOH A O   1 
HETATM 2100 O  O   . HOH L 6 .   ? -49.503 8.854   32.307  1.00 58.81 ? 668 HOH A O   1 
HETATM 2101 O  O   . HOH L 6 .   ? -26.194 19.540  6.236   1.00 39.97 ? 669 HOH A O   1 
HETATM 2102 O  O   . HOH L 6 .   ? -41.771 -4.396  9.085   1.00 46.58 ? 670 HOH A O   1 
HETATM 2103 O  O   . HOH L 6 .   ? -25.973 -17.342 -5.479  1.00 41.93 ? 671 HOH A O   1 
HETATM 2104 O  O   . HOH L 6 .   ? -12.439 3.714   1.587   1.00 65.45 ? 672 HOH A O   1 
HETATM 2105 O  O   . HOH L 6 .   ? -43.843 4.647   9.640   1.00 70.17 ? 673 HOH A O   1 
HETATM 2106 O  O   . HOH L 6 .   ? -31.909 3.454   -13.670 1.00 60.56 ? 674 HOH A O   1 
HETATM 2107 O  O   . HOH L 6 .   ? -26.405 30.766  11.586  1.00 38.79 ? 675 HOH A O   1 
HETATM 2108 O  O   . HOH L 6 .   ? -29.141 30.692  17.994  1.00 51.91 ? 676 HOH A O   1 
HETATM 2109 O  O   . HOH L 6 .   ? -13.831 5.107   3.317   1.00 49.69 ? 677 HOH A O   1 
HETATM 2110 O  O   . HOH L 6 .   ? -14.999 14.977  22.401  1.00 69.66 ? 678 HOH A O   1 
HETATM 2111 O  O   . HOH L 6 .   ? -35.707 -12.146 11.662  1.00 45.23 ? 679 HOH A O   1 
HETATM 2112 O  O   A HOH L 6 .   ? -35.585 -2.520  15.651  0.60 32.37 ? 680 HOH A O   1 
HETATM 2113 O  O   B HOH L 6 .   ? -35.061 -3.597  14.725  0.40 36.49 ? 680 HOH A O   1 
HETATM 2114 O  O   . HOH L 6 .   ? -19.249 -21.102 1.937   1.00 62.24 ? 681 HOH A O   1 
HETATM 2115 O  O   . HOH L 6 .   ? -24.417 -6.878  19.597  1.00 55.95 ? 682 HOH A O   1 
HETATM 2116 O  O   . HOH L 6 .   ? -22.612 -20.889 8.289   1.00 58.21 ? 683 HOH A O   1 
HETATM 2117 O  O   . HOH L 6 .   ? -43.923 -4.886  4.916   1.00 61.97 ? 684 HOH A O   1 
HETATM 2118 O  O   . HOH L 6 .   ? -43.956 22.312  16.528  1.00 44.43 ? 685 HOH A O   1 
HETATM 2119 O  O   . HOH L 6 .   ? -45.779 0.220   -3.015  1.00 50.18 ? 686 HOH A O   1 
HETATM 2120 O  O   . HOH L 6 .   ? -32.836 -2.981  16.336  1.00 52.90 ? 687 HOH A O   1 
HETATM 2121 O  O   . HOH L 6 .   ? -42.582 5.816   -11.521 1.00 50.39 ? 688 HOH A O   1 
HETATM 2122 O  O   . HOH L 6 .   ? -26.553 -1.947  20.515  1.00 64.37 ? 689 HOH A O   1 
HETATM 2123 O  O   . HOH L 6 .   ? -34.677 29.095  19.000  1.00 57.55 ? 690 HOH A O   1 
HETATM 2124 O  O   A HOH L 6 .   ? -36.371 -14.761 11.573  0.50 31.79 ? 691 HOH A O   1 
HETATM 2125 O  O   B HOH L 6 .   ? -38.148 -14.256 10.652  0.50 40.06 ? 691 HOH A O   1 
HETATM 2126 O  O   . HOH L 6 .   ? -23.700 30.192  13.009  1.00 62.89 ? 692 HOH A O   1 
HETATM 2127 O  O   . HOH L 6 .   ? -25.497 1.129   21.416  1.00 43.78 ? 693 HOH A O   1 
HETATM 2128 O  O   . HOH L 6 .   ? -44.444 17.217  -4.189  1.00 67.34 ? 694 HOH A O   1 
HETATM 2129 O  O   . HOH L 6 .   ? -31.589 1.895   33.048  1.00 37.44 ? 695 HOH A O   1 
HETATM 2130 O  O   . HOH L 6 .   ? -36.183 18.522  0.464   1.00 63.66 ? 696 HOH A O   1 
HETATM 2131 O  O   . HOH L 6 .   ? -35.586 19.273  7.293   1.00 41.20 ? 697 HOH A O   1 
HETATM 2132 O  O   . HOH L 6 .   ? -17.912 11.084  9.036   1.00 56.38 ? 698 HOH A O   1 
HETATM 2133 O  O   A HOH L 6 .   ? -18.937 7.509   7.020   0.60 32.58 ? 699 HOH A O   1 
HETATM 2134 O  O   B HOH L 6 .   ? -17.574 6.452   6.786   0.40 39.97 ? 699 HOH A O   1 
HETATM 2135 O  O   . HOH L 6 .   ? -27.965 14.364  -14.013 1.00 44.30 ? 700 HOH A O   1 
HETATM 2136 O  O   . HOH L 6 .   ? -45.653 -2.565  -2.367  1.00 36.75 ? 701 HOH A O   1 
HETATM 2137 O  O   . HOH L 6 .   ? -37.155 -9.505  11.655  1.00 55.76 ? 702 HOH A O   1 
HETATM 2138 O  O   . HOH L 6 .   ? -28.428 -10.089 15.856  1.00 64.33 ? 703 HOH A O   1 
HETATM 2139 O  O   . HOH L 6 .   ? -43.376 5.989   7.312   1.00 47.73 ? 704 HOH A O   1 
HETATM 2140 O  O   . HOH L 6 .   ? -15.966 24.254  16.325  1.00 58.59 ? 705 HOH A O   1 
HETATM 2141 O  O   . HOH L 6 .   ? -35.231 11.368  33.015  1.00 57.78 ? 706 HOH A O   1 
HETATM 2142 O  O   . HOH L 6 .   ? -45.135 4.694   37.195  1.00 44.63 ? 707 HOH A O   1 
HETATM 2143 O  O   . HOH L 6 .   ? -17.831 9.540   6.454   1.00 46.06 ? 708 HOH A O   1 
HETATM 2144 O  O   . HOH L 6 .   ? -23.263 15.090  26.525  1.00 62.60 ? 709 HOH A O   1 
HETATM 2145 O  O   . HOH L 6 .   ? -21.524 2.424   18.821  1.00 38.15 ? 710 HOH A O   1 
HETATM 2146 O  O   . HOH L 6 .   ? -21.848 32.952  15.993  1.00 66.91 ? 711 HOH A O   1 
HETATM 2147 O  O   . HOH L 6 .   ? -20.921 5.061   18.070  1.00 54.39 ? 712 HOH A O   1 
HETATM 2148 O  O   . HOH L 6 .   ? -43.769 -4.797  -2.071  1.00 34.10 ? 713 HOH A O   1 
HETATM 2149 O  O   . HOH L 6 .   ? -27.306 -11.536 12.972  1.00 54.38 ? 714 HOH A O   1 
HETATM 2150 O  O   . HOH L 6 .   ? -47.882 1.946   -0.502  1.00 50.80 ? 715 HOH A O   1 
HETATM 2151 O  O   . HOH L 6 .   ? -21.312 6.701   21.183  1.00 45.84 ? 716 HOH A O   1 
HETATM 2152 O  O   . HOH L 6 .   ? -19.132 7.457   12.522  1.00 48.27 ? 717 HOH A O   1 
HETATM 2153 O  O   . HOH L 6 .   ? -23.605 -5.028  21.251  1.00 60.68 ? 718 HOH A O   1 
HETATM 2154 O  O   . HOH L 6 .   ? -24.351 3.121   23.008  1.00 41.87 ? 719 HOH A O   1 
HETATM 2155 O  O   . HOH L 6 .   ? -32.404 5.652   36.083  1.00 57.66 ? 720 HOH A O   1 
HETATM 2156 O  O   . HOH L 6 .   ? -24.598 1.805   25.225  1.00 47.48 ? 721 HOH A O   1 
HETATM 2157 O  O   . HOH L 6 .   ? -23.783 11.595  -7.183  1.00 57.78 ? 722 HOH A O   1 
HETATM 2158 O  O   A HOH L 6 .   ? -19.040 28.642  13.675  0.70 41.55 ? 723 HOH A O   1 
HETATM 2159 O  O   B HOH L 6 .   ? -20.481 29.557  12.730  0.30 30.22 ? 723 HOH A O   1 
HETATM 2160 O  O   . HOH L 6 .   ? -16.932 -0.918  -6.275  1.00 61.31 ? 724 HOH A O   1 
HETATM 2161 O  O   . HOH L 6 .   ? -33.360 27.025  22.996  1.00 56.85 ? 725 HOH A O   1 
HETATM 2162 O  O   . HOH L 6 .   ? -38.146 25.527  22.195  1.00 48.42 ? 726 HOH A O   1 
HETATM 2163 O  O   . HOH L 6 .   ? -17.728 -16.837 -2.080  1.00 59.13 ? 727 HOH A O   1 
HETATM 2164 O  O   . HOH L 6 .   ? -49.052 2.920   32.961  1.00 56.91 ? 728 HOH A O   1 
HETATM 2165 O  O   . HOH L 6 .   ? -47.744 4.498   35.748  1.00 54.39 ? 729 HOH A O   1 
HETATM 2166 O  O   . HOH L 6 .   ? -14.029 -14.688 7.910   1.00 68.62 ? 730 HOH A O   1 
HETATM 2167 O  O   . HOH L 6 .   ? -19.287 -0.227  -7.614  1.00 62.39 ? 731 HOH A O   1 
HETATM 2168 O  O   . HOH L 6 .   ? -22.521 2.519   29.050  1.00 67.19 ? 732 HOH A O   1 
HETATM 2169 O  O   . HOH L 6 .   ? -49.641 2.354   3.540   1.00 66.02 ? 733 HOH A O   1 
HETATM 2170 O  O   . HOH L 6 .   ? -50.770 4.918   8.444   1.00 67.13 ? 734 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . GLN A 3   ? 0.7623 0.7283 0.6815 -0.0808 -0.0532 -0.0468 3   GLN A N   
2    C  CA  . GLN A 3   ? 0.7288 0.6912 0.6493 -0.0791 -0.0517 -0.0426 3   GLN A CA  
3    C  C   . GLN A 3   ? 0.6485 0.5984 0.5617 -0.0768 -0.0503 -0.0366 3   GLN A C   
4    O  O   . GLN A 3   ? 0.7247 0.6694 0.6332 -0.0743 -0.0510 -0.0353 3   GLN A O   
5    C  CB  . GLN A 3   ? 0.8082 0.7770 0.7364 -0.0738 -0.0540 -0.0427 3   GLN A CB  
6    N  N   . GLU A 4   ? 0.6011 0.5464 0.5133 -0.0775 -0.0483 -0.0331 4   GLU A N   
7    C  CA  . GLU A 4   ? 0.5570 0.4914 0.4631 -0.0752 -0.0468 -0.0273 4   GLU A CA  
8    C  C   . GLU A 4   ? 0.5336 0.4667 0.4424 -0.0683 -0.0483 -0.0237 4   GLU A C   
9    O  O   . GLU A 4   ? 0.5194 0.4579 0.4348 -0.0661 -0.0497 -0.0237 4   GLU A O   
10   C  CB  . GLU A 4   ? 0.5642 0.4960 0.4695 -0.0783 -0.0446 -0.0254 4   GLU A CB  
11   C  CG  . GLU A 4   ? 0.6488 0.5823 0.5514 -0.0854 -0.0430 -0.0294 4   GLU A CG  
12   C  CD  . GLU A 4   ? 0.6751 0.6047 0.5752 -0.0888 -0.0407 -0.0275 4   GLU A CD  
13   O  OE1 . GLU A 4   ? 0.6761 0.5970 0.5716 -0.0867 -0.0396 -0.0225 4   GLU A OE1 
14   O  OE2 . GLU A 4   ? 0.8323 0.7671 0.7344 -0.0934 -0.0399 -0.0309 4   GLU A OE2 
15   N  N   . GLN A 5   ? 0.4859 0.4114 0.3892 -0.0651 -0.0480 -0.0205 5   GLN A N   
16   C  CA  . GLN A 5   ? 0.4978 0.4217 0.4031 -0.0588 -0.0492 -0.0170 5   GLN A CA  
17   C  C   . GLN A 5   ? 0.4374 0.3511 0.3365 -0.0566 -0.0470 -0.0115 5   GLN A C   
18   O  O   . GLN A 5   ? 0.4274 0.3349 0.3194 -0.0587 -0.0455 -0.0114 5   GLN A O   
19   C  CB  . GLN A 5   ? 0.5657 0.4912 0.4702 -0.0559 -0.0514 -0.0192 5   GLN A CB  
20   C  CG  . GLN A 5   ? 0.6276 0.5635 0.5378 -0.0571 -0.0539 -0.0250 5   GLN A CG  
21   C  CD  . GLN A 5   ? 0.6809 0.6174 0.5898 -0.0530 -0.0564 -0.0263 5   GLN A CD  
22   O  OE1 . GLN A 5   ? 0.7546 0.6895 0.6648 -0.0476 -0.0575 -0.0235 5   GLN A OE1 
23   N  NE2 . GLN A 5   ? 0.7337 0.6715 0.6393 -0.0557 -0.0573 -0.0301 5   GLN A NE2 
24   N  N   . LEU A 6   ? 0.4192 0.3312 0.3211 -0.0520 -0.0470 -0.0071 6   LEU A N   
25   C  CA  . LEU A 6   ? 0.4075 0.3110 0.3044 -0.0486 -0.0452 -0.0019 6   LEU A CA  
26   C  C   . LEU A 6   ? 0.4366 0.3405 0.3354 -0.0430 -0.0466 -0.0004 6   LEU A C   
27   O  O   . LEU A 6   ? 0.4539 0.3620 0.3590 -0.0410 -0.0479 0.0003  6   LEU A O   
28   C  CB  . LEU A 6   ? 0.4158 0.3176 0.3153 -0.0483 -0.0437 0.0025  6   LEU A CB  
29   C  CG  . LEU A 6   ? 0.4235 0.3252 0.3218 -0.0536 -0.0425 0.0014  6   LEU A CG  
30   C  CD1 . LEU A 6   ? 0.3770 0.2777 0.2785 -0.0529 -0.0417 0.0058  6   LEU A CD1 
31   C  CD2 . LEU A 6   ? 0.4267 0.3210 0.3160 -0.0556 -0.0406 0.0011  6   LEU A CD2 
32   N  N   . GLN A 7   ? 0.4252 0.3240 0.3179 -0.0408 -0.0464 -0.0001 7   GLN A N   
33   C  CA  . GLN A 7   ? 0.4296 0.3286 0.3229 -0.0358 -0.0480 0.0004  7   GLN A CA  
34   C  C   . GLN A 7   ? 0.4308 0.3219 0.3203 -0.0314 -0.0457 0.0063  7   GLN A C   
35   O  O   . GLN A 7   ? 0.4310 0.3150 0.3133 -0.0313 -0.0436 0.0079  7   GLN A O   
36   C  CB  . GLN A 7   ? 0.4837 0.3834 0.3727 -0.0363 -0.0499 -0.0040 7   GLN A CB  
37   C  CG  . GLN A 7   ? 0.5977 0.4952 0.4846 -0.0309 -0.0513 -0.0030 7   GLN A CG  
38   C  CD  . GLN A 7   ? 0.6377 0.5364 0.5206 -0.0315 -0.0536 -0.0077 7   GLN A CD  
39   O  OE1 . GLN A 7   ? 0.6833 0.5900 0.5704 -0.0341 -0.0561 -0.0127 7   GLN A OE1 
40   N  NE2 . GLN A 7   ? 0.7019 0.5929 0.5766 -0.0294 -0.0527 -0.0062 7   GLN A NE2 
41   N  N   . GLN A 8   ? 0.3847 0.2771 0.2790 -0.0278 -0.0459 0.0095  8   GLN A N   
42   C  CA  . GLN A 8   ? 0.3992 0.2855 0.2914 -0.0236 -0.0436 0.0151  8   GLN A CA  
43   C  C   . GLN A 8   ? 0.4231 0.3087 0.3150 -0.0189 -0.0448 0.0159  8   GLN A C   
44   O  O   . GLN A 8   ? 0.4314 0.3225 0.3284 -0.0185 -0.0474 0.0137  8   GLN A O   
45   C  CB  . GLN A 8   ? 0.4005 0.2890 0.2993 -0.0237 -0.0426 0.0189  8   GLN A CB  
46   C  CG  . GLN A 8   ? 0.4000 0.2885 0.2990 -0.0278 -0.0413 0.0191  8   GLN A CG  
47   C  CD  . GLN A 8   ? 0.4050 0.2955 0.3102 -0.0277 -0.0405 0.0230  8   GLN A CD  
48   O  OE1 . GLN A 8   ? 0.3815 0.2775 0.2925 -0.0301 -0.0422 0.0214  8   GLN A OE1 
49   N  NE2 . GLN A 8   ? 0.4187 0.3049 0.3229 -0.0246 -0.0381 0.0283  8   GLN A NE2 
50   N  N   . PRO A 9   ? 0.5006 0.3792 0.3866 -0.0150 -0.0429 0.0193  9   PRO A N   
51   C  CA  . PRO A 9   ? 0.4832 0.3600 0.3680 -0.0103 -0.0436 0.0207  9   PRO A CA  
52   C  C   . PRO A 9   ? 0.5155 0.3956 0.4079 -0.0090 -0.0438 0.0235  9   PRO A C   
53   O  O   . PRO A 9   ? 0.4820 0.3636 0.3792 -0.0105 -0.0423 0.0263  9   PRO A O   
54   C  CB  . PRO A 9   ? 0.5277 0.3961 0.4053 -0.0071 -0.0403 0.0248  9   PRO A CB  
55   C  CG  . PRO A 9   ? 0.5957 0.4612 0.4682 -0.0103 -0.0391 0.0231  9   PRO A CG  
56   C  CD  . PRO A 9   ? 0.5479 0.4194 0.4275 -0.0147 -0.0396 0.0221  9   PRO A CD  
57   N  N   . GLY A 10  ? 0.4896 0.3706 0.3830 -0.0061 -0.0459 0.0229  10  GLY A N   
58   C  CA  . GLY A 10  ? 0.4476 0.3313 0.3477 -0.0052 -0.0463 0.0251  10  GLY A CA  
59   C  C   . GLY A 10  ? 0.5037 0.3832 0.4045 -0.0031 -0.0429 0.0315  10  GLY A C   
60   O  O   . GLY A 10  ? 0.4767 0.3591 0.3841 -0.0045 -0.0424 0.0338  10  GLY A O   
61   N  N   . THR A 11  ? 0.5115 0.3845 0.4058 0.0004  -0.0406 0.0344  11  THR A N   
62   C  CA  . THR A 11  ? 0.5072 0.3766 0.4023 0.0029  -0.0373 0.0404  11  THR A CA  
63   C  C   . THR A 11  ? 0.5394 0.4024 0.4273 0.0052  -0.0338 0.0431  11  THR A C   
64   O  O   . THR A 11  ? 0.5428 0.4019 0.4230 0.0065  -0.0343 0.0408  11  THR A O   
65   C  CB  . THR A 11  ? 0.5185 0.3856 0.4128 0.0064  -0.0380 0.0418  11  THR A CB  
66   O  OG1 . THR A 11  ? 0.5412 0.4053 0.4283 0.0086  -0.0400 0.0384  11  THR A OG1 
67   C  CG2 . THR A 11  ? 0.5359 0.4078 0.4370 0.0051  -0.0409 0.0403  11  THR A CG2 
68   N  N   . GLU A 12  ? 0.4820 0.3439 0.3724 0.0061  -0.0302 0.0483  12  GLU A N   
69   C  CA  . GLU A 12  ? 0.5064 0.3618 0.3902 0.0092  -0.0264 0.0516  12  GLU A CA  
70   C  C   . GLU A 12  ? 0.5620 0.4166 0.4491 0.0117  -0.0235 0.0571  12  GLU A C   
71   O  O   . GLU A 12  ? 0.4660 0.3252 0.3611 0.0099  -0.0229 0.0595  12  GLU A O   
72   C  CB  . GLU A 12  ? 0.4670 0.3220 0.3503 0.0078  -0.0241 0.0527  12  GLU A CB  
73   C  CG  . GLU A 12  ? 0.5954 0.4502 0.4744 0.0049  -0.0264 0.0475  12  GLU A CG  
74   C  CD  . GLU A 12  ? 0.7899 0.6385 0.6586 0.0067  -0.0267 0.0449  12  GLU A CD  
75   O  OE1 . GLU A 12  ? 0.7486 0.5913 0.6115 0.0108  -0.0245 0.0475  12  GLU A OE1 
76   O  OE2 . GLU A 12  ? 0.8459 0.6954 0.7120 0.0039  -0.0293 0.0400  12  GLU A OE2 
77   N  N   . LEU A 13  ? 0.5181 0.3669 0.3988 0.0156  -0.0219 0.0588  13  LEU A N   
78   C  CA  . LEU A 13  ? 0.5004 0.3477 0.3833 0.0180  -0.0186 0.0641  13  LEU A CA  
79   C  C   . LEU A 13  ? 0.5271 0.3698 0.4053 0.0209  -0.0137 0.0681  13  LEU A C   
80   O  O   . LEU A 13  ? 0.5142 0.3505 0.3830 0.0235  -0.0128 0.0670  13  LEU A O   
81   C  CB  . LEU A 13  ? 0.5027 0.3464 0.3813 0.0204  -0.0203 0.0632  13  LEU A CB  
82   C  CG  . LEU A 13  ? 0.4988 0.3404 0.3791 0.0224  -0.0172 0.0684  13  LEU A CG  
83   C  CD1 . LEU A 13  ? 0.4774 0.3253 0.3685 0.0193  -0.0178 0.0702  13  LEU A CD1 
84   C  CD2 . LEU A 13  ? 0.5246 0.3604 0.3980 0.0255  -0.0184 0.0678  13  LEU A CD2 
85   N  N   . VAL A 14  ? 0.4689 0.3148 0.3535 0.0205  -0.0105 0.0723  14  VAL A N   
86   C  CA  . VAL A 14  ? 0.4748 0.3175 0.3558 0.0229  -0.0061 0.0753  14  VAL A CA  
87   C  C   . VAL A 14  ? 0.5249 0.3694 0.4114 0.0247  -0.0018 0.0813  14  VAL A C   
88   O  O   . VAL A 14  ? 0.5138 0.3634 0.4086 0.0228  -0.0025 0.0830  14  VAL A O   
89   C  CB  . VAL A 14  ? 0.4849 0.3310 0.3685 0.0202  -0.0073 0.0734  14  VAL A CB  
90   C  CG1 . VAL A 14  ? 0.5441 0.3879 0.4216 0.0183  -0.0110 0.0675  14  VAL A CG1 
91   C  CG2 . VAL A 14  ? 0.4722 0.3266 0.3674 0.0165  -0.0090 0.0743  14  VAL A CG2 
92   N  N   . LYS A 15  ? 0.5487 0.3891 0.4304 0.0283  0.0028  0.0844  15  LYS A N   
93   C  CA  . LYS A 15  ? 0.5588 0.4006 0.4446 0.0306  0.0077  0.0901  15  LYS A CA  
94   C  C   . LYS A 15  ? 0.5167 0.3649 0.4108 0.0296  0.0092  0.0927  15  LYS A C   
95   O  O   . LYS A 15  ? 0.5357 0.3838 0.4282 0.0289  0.0081  0.0906  15  LYS A O   
96   C  CB  . LYS A 15  ? 0.6269 0.4607 0.5025 0.0355  0.0123  0.0921  15  LYS A CB  
97   C  CG  . LYS A 15  ? 0.6184 0.4439 0.4826 0.0375  0.0110  0.0893  15  LYS A CG  
98   C  CD  . LYS A 15  ? 0.6792 0.4963 0.5328 0.0424  0.0157  0.0914  15  LYS A CD  
99   C  CE  . LYS A 15  ? 0.7116 0.5281 0.5667 0.0447  0.0199  0.0961  15  LYS A CE  
100  N  NZ  . LYS A 15  ? 0.7873 0.5947 0.6308 0.0494  0.0240  0.0978  15  LYS A NZ  
101  N  N   . PRO A 16  ? 0.4930 0.3469 0.3963 0.0293  0.0117  0.0972  16  PRO A N   
102  C  CA  . PRO A 16  ? 0.5171 0.3774 0.4282 0.0291  0.0134  0.1001  16  PRO A CA  
103  C  C   . PRO A 16  ? 0.5661 0.4214 0.4700 0.0334  0.0173  0.1012  16  PRO A C   
104  O  O   . PRO A 16  ? 0.5674 0.4159 0.4628 0.0371  0.0205  0.1021  16  PRO A O   
105  C  CB  . PRO A 16  ? 0.5438 0.4101 0.4644 0.0288  0.0162  0.1050  16  PRO A CB  
106  C  CG  . PRO A 16  ? 0.5395 0.4035 0.4590 0.0271  0.0142  0.1037  16  PRO A CG  
107  C  CD  . PRO A 16  ? 0.5235 0.3788 0.4307 0.0287  0.0124  0.0995  16  PRO A CD  
108  N  N   . GLY A 17  ? 0.5518 0.4099 0.4581 0.0329  0.0166  0.1009  17  GLY A N   
109  C  CA  . GLY A 17  ? 0.5740 0.4273 0.4738 0.0371  0.0202  0.1023  17  GLY A CA  
110  C  C   . GLY A 17  ? 0.5643 0.4087 0.4518 0.0375  0.0184  0.0977  17  GLY A C   
111  O  O   . GLY A 17  ? 0.6150 0.4553 0.4971 0.0399  0.0203  0.0979  17  GLY A O   
112  N  N   . ALA A 18  ? 0.5765 0.4178 0.4594 0.0351  0.0148  0.0935  18  ALA A N   
113  C  CA  . ALA A 18  ? 0.5396 0.3735 0.4118 0.0345  0.0126  0.0887  18  ALA A CA  
114  C  C   . ALA A 18  ? 0.5656 0.4027 0.4408 0.0306  0.0090  0.0858  18  ALA A C   
115  O  O   . ALA A 18  ? 0.5539 0.3986 0.4390 0.0286  0.0081  0.0875  18  ALA A O   
116  C  CB  . ALA A 18  ? 0.5336 0.3645 0.4011 0.0334  0.0098  0.0854  18  ALA A CB  
117  N  N   A SER A 19  ? 0.5604 0.3911 0.4263 0.0297  0.0072  0.0816  19  SER A N   
118  N  N   B SER A 19  ? 0.5524 0.3833 0.4185 0.0294  0.0070  0.0814  19  SER A N   
119  C  CA  A SER A 19  ? 0.5732 0.4060 0.4402 0.0251  0.0033  0.0778  19  SER A CA  
120  C  CA  B SER A 19  ? 0.5482 0.3808 0.4151 0.0252  0.0034  0.0778  19  SER A CA  
121  C  C   A SER A 19  ? 0.5691 0.4013 0.4333 0.0219  -0.0008 0.0726  19  SER A C   
122  C  C   B SER A 19  ? 0.5553 0.3864 0.4180 0.0219  -0.0007 0.0723  19  SER A C   
123  O  O   A SER A 19  ? 0.5402 0.3681 0.3986 0.0238  -0.0005 0.0717  19  SER A O   
124  O  O   B SER A 19  ? 0.5667 0.3916 0.4210 0.0239  -0.0003 0.0708  19  SER A O   
125  C  CB  A SER A 19  ? 0.6320 0.4583 0.4910 0.0259  0.0045  0.0769  19  SER A CB  
126  C  CB  B SER A 19  ? 0.5606 0.3868 0.4198 0.0268  0.0053  0.0777  19  SER A CB  
127  O  OG  A SER A 19  ? 0.6454 0.4728 0.5076 0.0292  0.0081  0.0816  19  SER A OG  
128  O  OG  B SER A 19  ? 0.5327 0.3495 0.3797 0.0287  0.0062  0.0755  19  SER A OG  
129  N  N   . VAL A 20  ? 0.5308 0.3674 0.3990 0.0172  -0.0047 0.0692  20  VAL A N   
130  C  CA  . VAL A 20  ? 0.5141 0.3507 0.3797 0.0142  -0.0086 0.0639  20  VAL A CA  
131  C  C   . VAL A 20  ? 0.5040 0.3406 0.3677 0.0100  -0.0110 0.0600  20  VAL A C   
132  O  O   . VAL A 20  ? 0.4951 0.3348 0.3635 0.0083  -0.0109 0.0613  20  VAL A O   
133  C  CB  . VAL A 20  ? 0.5171 0.3607 0.3912 0.0126  -0.0112 0.0636  20  VAL A CB  
134  C  CG1 . VAL A 20  ? 0.5220 0.3735 0.4068 0.0094  -0.0127 0.0646  20  VAL A CG1 
135  C  CG2 . VAL A 20  ? 0.5160 0.3592 0.3867 0.0106  -0.0151 0.0583  20  VAL A CG2 
136  N  N   . ARG A 21  ? 0.5163 0.3493 0.3729 0.0082  -0.0132 0.0552  21  ARG A N   
137  C  CA  . ARG A 21  ? 0.5265 0.3596 0.3813 0.0036  -0.0153 0.0513  21  ARG A CA  
138  C  C   . ARG A 21  ? 0.5161 0.3558 0.3758 -0.0003 -0.0196 0.0468  21  ARG A C   
139  O  O   . ARG A 21  ? 0.5261 0.3653 0.3832 0.0001  -0.0214 0.0441  21  ARG A O   
140  C  CB  . ARG A 21  ? 0.5914 0.4155 0.4341 0.0039  -0.0144 0.0489  21  ARG A CB  
141  C  CG  . ARG A 21  ? 0.6415 0.4648 0.4824 -0.0005 -0.0154 0.0463  21  ARG A CG  
142  C  CD  . ARG A 21  ? 0.7370 0.5501 0.5655 -0.0005 -0.0139 0.0447  21  ARG A CD  
143  N  NE  . ARG A 21  ? 0.7756 0.5866 0.5987 -0.0011 -0.0160 0.0407  21  ARG A NE  
144  C  CZ  . ARG A 21  ? 0.8148 0.6211 0.6299 -0.0043 -0.0174 0.0363  21  ARG A CZ  
145  N  NH1 . ARG A 21  ? 0.8709 0.6716 0.6803 -0.0066 -0.0161 0.0357  21  ARG A NH1 
146  N  NH2 . ARG A 21  ? 0.8276 0.6350 0.6406 -0.0052 -0.0201 0.0325  21  ARG A NH2 
147  N  N   . LEU A 22  ? 0.4958 0.3418 0.3629 -0.0040 -0.0213 0.0460  22  LEU A N   
148  C  CA  . LEU A 22  ? 0.4894 0.3419 0.3615 -0.0079 -0.0251 0.0417  22  LEU A CA  
149  C  C   . LEU A 22  ? 0.4809 0.3321 0.3481 -0.0123 -0.0266 0.0368  22  LEU A C   
150  O  O   . LEU A 22  ? 0.4945 0.3419 0.3579 -0.0136 -0.0251 0.0374  22  LEU A O   
151  C  CB  . LEU A 22  ? 0.4483 0.3082 0.3308 -0.0095 -0.0260 0.0435  22  LEU A CB  
152  C  CG  . LEU A 22  ? 0.4587 0.3202 0.3467 -0.0058 -0.0243 0.0486  22  LEU A CG  
153  C  CD1 . LEU A 22  ? 0.4701 0.3392 0.3682 -0.0083 -0.0261 0.0493  22  LEU A CD1 
154  C  CD2 . LEU A 22  ? 0.4734 0.3335 0.3593 -0.0030 -0.0247 0.0482  22  LEU A CD2 
155  N  N   . SER A 23  ? 0.4683 0.3227 0.3355 -0.0145 -0.0297 0.0319  23  SER A N   
156  C  CA  . SER A 23  ? 0.4656 0.3195 0.3287 -0.0191 -0.0311 0.0270  23  SER A CA  
157  C  C   . SER A 23  ? 0.4580 0.3205 0.3286 -0.0234 -0.0339 0.0235  23  SER A C   
158  O  O   . SER A 23  ? 0.4491 0.3177 0.3268 -0.0226 -0.0357 0.0233  23  SER A O   
159  C  CB  . SER A 23  ? 0.4920 0.3418 0.3474 -0.0186 -0.0320 0.0237  23  SER A CB  
160  O  OG  . SER A 23  ? 0.5369 0.3907 0.3956 -0.0163 -0.0343 0.0226  23  SER A OG  
161  N  N   . CYS A 24  ? 0.4549 0.3173 0.3231 -0.0281 -0.0341 0.0204  24  CYS A N   
162  C  CA  . CYS A 24  ? 0.4557 0.3256 0.3298 -0.0327 -0.0363 0.0166  24  CYS A CA  
163  C  C   . CYS A 24  ? 0.4870 0.3556 0.3553 -0.0371 -0.0371 0.0116  24  CYS A C   
164  O  O   . CYS A 24  ? 0.4657 0.3294 0.3288 -0.0399 -0.0354 0.0116  24  CYS A O   
165  C  CB  . CYS A 24  ? 0.4474 0.3185 0.3255 -0.0343 -0.0352 0.0194  24  CYS A CB  
166  S  SG  . CYS A 24  ? 0.4892 0.3681 0.3727 -0.0404 -0.0373 0.0149  24  CYS A SG  
167  N  N   . LYS A 25  ? 0.4518 0.3243 0.3206 -0.0374 -0.0396 0.0074  25  LYS A N   
168  C  CA  . LYS A 25  ? 0.4851 0.3577 0.3493 -0.0418 -0.0407 0.0022  25  LYS A CA  
169  C  C   . LYS A 25  ? 0.4920 0.3726 0.3619 -0.0472 -0.0420 -0.0018 25  LYS A C   
170  O  O   . LYS A 25  ? 0.4851 0.3741 0.3629 -0.0467 -0.0441 -0.0034 25  LYS A O   
171  C  CB  . LYS A 25  ? 0.4825 0.3554 0.3443 -0.0391 -0.0428 0.0000  25  LYS A CB  
172  C  CG  . LYS A 25  ? 0.5549 0.4278 0.4117 -0.0435 -0.0441 -0.0054 25  LYS A CG  
173  C  CD  . LYS A 25  ? 0.5799 0.4553 0.4361 -0.0408 -0.0471 -0.0081 25  LYS A CD  
174  N  N   . THR A 26  ? 0.4406 0.3183 0.3060 -0.0523 -0.0406 -0.0034 26  THR A N   
175  C  CA  . THR A 26  ? 0.4505 0.3348 0.3208 -0.0574 -0.0411 -0.0065 26  THR A CA  
176  C  C   . THR A 26  ? 0.4642 0.3527 0.3332 -0.0619 -0.0427 -0.0127 26  THR A C   
177  O  O   . THR A 26  ? 0.4655 0.3486 0.3272 -0.0625 -0.0426 -0.0139 26  THR A O   
178  C  CB  . THR A 26  ? 0.4503 0.3294 0.3174 -0.0603 -0.0385 -0.0041 26  THR A CB  
179  O  OG1 . THR A 26  ? 0.4600 0.3321 0.3179 -0.0639 -0.0372 -0.0060 26  THR A OG1 
180  C  CG2 . THR A 26  ? 0.4569 0.3304 0.3234 -0.0555 -0.0368 0.0021  26  THR A CG2 
181  N  N   . SER A 27  ? 0.4573 0.3553 0.3332 -0.0653 -0.0440 -0.0164 27  SER A N   
182  C  CA  . SER A 27  ? 0.4833 0.3865 0.3590 -0.0704 -0.0452 -0.0224 27  SER A CA  
183  C  C   . SER A 27  ? 0.4863 0.3975 0.3681 -0.0753 -0.0449 -0.0253 27  SER A C   
184  O  O   . SER A 27  ? 0.4662 0.3805 0.3536 -0.0739 -0.0448 -0.0233 27  SER A O   
185  C  CB  . SER A 27  ? 0.5222 0.4311 0.4006 -0.0678 -0.0483 -0.0255 27  SER A CB  
186  O  OG  . SER A 27  ? 0.5369 0.4528 0.4237 -0.0636 -0.0501 -0.0248 27  SER A OG  
187  N  N   . GLY A 28  ? 0.4713 0.3854 0.3514 -0.0813 -0.0448 -0.0301 28  GLY A N   
188  C  CA  . GLY A 28  ? 0.4901 0.4136 0.3768 -0.0857 -0.0448 -0.0337 28  GLY A CA  
189  C  C   . GLY A 28  ? 0.4804 0.3989 0.3632 -0.0905 -0.0417 -0.0323 28  GLY A C   
190  O  O   . GLY A 28  ? 0.4967 0.4220 0.3841 -0.0942 -0.0413 -0.0350 28  GLY A O   
191  N  N   . TYR A 29  ? 0.4935 0.4002 0.3679 -0.0899 -0.0397 -0.0281 29  TYR A N   
192  C  CA  . TYR A 29  ? 0.4574 0.3576 0.3267 -0.0939 -0.0369 -0.0263 29  TYR A CA  
193  C  C   . TYR A 29  ? 0.4799 0.3668 0.3382 -0.0932 -0.0351 -0.0231 29  TYR A C   
194  O  O   . TYR A 29  ? 0.4739 0.3573 0.3299 -0.0889 -0.0360 -0.0217 29  TYR A O   
195  C  CB  . TYR A 29  ? 0.4313 0.3330 0.3055 -0.0911 -0.0367 -0.0228 29  TYR A CB  
196  C  CG  . TYR A 29  ? 0.4588 0.3541 0.3318 -0.0845 -0.0367 -0.0168 29  TYR A CG  
197  C  CD1 . TYR A 29  ? 0.4239 0.3232 0.3025 -0.0787 -0.0388 -0.0157 29  TYR A CD1 
198  C  CD2 . TYR A 29  ? 0.4497 0.3345 0.3154 -0.0839 -0.0346 -0.0124 29  TYR A CD2 
199  C  CE1 . TYR A 29  ? 0.4234 0.3171 0.3010 -0.0731 -0.0385 -0.0103 29  TYR A CE1 
200  C  CE2 . TYR A 29  ? 0.4484 0.3281 0.3136 -0.0779 -0.0344 -0.0071 29  TYR A CE2 
201  C  CZ  . TYR A 29  ? 0.4405 0.3250 0.3120 -0.0727 -0.0362 -0.0060 29  TYR A CZ  
202  O  OH  . TYR A 29  ? 0.4392 0.3185 0.3098 -0.0672 -0.0356 -0.0007 29  TYR A OH  
203  N  N   . THR A 30  ? 0.4937 0.3725 0.3447 -0.0971 -0.0326 -0.0218 30  THR A N   
204  C  CA  . THR A 30  ? 0.4749 0.3404 0.3148 -0.0964 -0.0307 -0.0189 30  THR A CA  
205  C  C   . THR A 30  ? 0.4743 0.3341 0.3138 -0.0894 -0.0303 -0.0127 30  THR A C   
206  O  O   . THR A 30  ? 0.4783 0.3364 0.3183 -0.0891 -0.0293 -0.0097 30  THR A O   
207  C  CB  . THR A 30  ? 0.5203 0.3780 0.3519 -0.1024 -0.0281 -0.0192 30  THR A CB  
208  O  OG1 . THR A 30  ? 0.5410 0.4058 0.3746 -0.1090 -0.0285 -0.0251 30  THR A OG1 
209  C  CG2 . THR A 30  ? 0.5294 0.3729 0.3489 -0.1014 -0.0264 -0.0166 30  THR A CG2 
210  N  N   . PHE A 31  ? 0.4918 0.3484 0.3295 -0.0842 -0.0310 -0.0109 31  PHE A N   
211  C  CA  . PHE A 31  ? 0.4614 0.3141 0.2998 -0.0772 -0.0306 -0.0052 31  PHE A CA  
212  C  C   . PHE A 31  ? 0.5245 0.3670 0.3558 -0.0769 -0.0281 -0.0011 31  PHE A C   
213  O  O   . PHE A 31  ? 0.4741 0.3171 0.3090 -0.0735 -0.0278 0.0030  31  PHE A O   
214  C  CB  . PHE A 31  ? 0.4875 0.3358 0.3217 -0.0732 -0.0310 -0.0048 31  PHE A CB  
215  C  CG  . PHE A 31  ? 0.4856 0.3284 0.3187 -0.0660 -0.0300 0.0009  31  PHE A CG  
216  C  CD1 . PHE A 31  ? 0.5107 0.3602 0.3530 -0.0616 -0.0310 0.0037  31  PHE A CD1 
217  C  CD2 . PHE A 31  ? 0.5154 0.3464 0.3384 -0.0637 -0.0279 0.0035  31  PHE A CD2 
218  C  CE1 . PHE A 31  ? 0.5411 0.3863 0.3830 -0.0553 -0.0299 0.0090  31  PHE A CE1 
219  C  CE2 . PHE A 31  ? 0.5059 0.3327 0.3284 -0.0569 -0.0267 0.0087  31  PHE A CE2 
220  C  CZ  . PHE A 31  ? 0.5272 0.3615 0.3596 -0.0529 -0.0277 0.0115  31  PHE A CZ  
221  N  N   . ALA A 32  ? 0.5120 0.3452 0.3328 -0.0807 -0.0264 -0.0023 32  ALA A N   
222  C  CA  . ALA A 32  ? 0.5064 0.3282 0.3186 -0.0799 -0.0240 0.0015  32  ALA A CA  
223  C  C   . ALA A 32  ? 0.5058 0.3298 0.3211 -0.0818 -0.0236 0.0030  32  ALA A C   
224  O  O   . ALA A 32  ? 0.5532 0.3697 0.3640 -0.0790 -0.0222 0.0074  32  ALA A O   
225  C  CB  . ALA A 32  ? 0.5210 0.3324 0.3210 -0.0848 -0.0224 -0.0009 32  ALA A CB  
226  N  N   . SER A 33  ? 0.4730 0.3069 0.2955 -0.0861 -0.0248 -0.0004 33  SER A N   
227  C  CA  . SER A 33  ? 0.4668 0.3008 0.2892 -0.0895 -0.0241 0.0000  33  SER A CA  
228  C  C   . SER A 33  ? 0.4528 0.2943 0.2848 -0.0862 -0.0255 0.0027  33  SER A C   
229  O  O   . SER A 33  ? 0.4422 0.2835 0.2738 -0.0889 -0.0250 0.0033  33  SER A O   
230  C  CB  . SER A 33  ? 0.4938 0.3319 0.3159 -0.0973 -0.0238 -0.0054 33  SER A CB  
231  O  OG  . SER A 33  ? 0.5184 0.3478 0.3302 -0.1012 -0.0223 -0.0075 33  SER A OG  
232  N  N   . TYR A 34  ? 0.4704 0.3178 0.3103 -0.0807 -0.0271 0.0045  34  TYR A N   
233  C  CA  . TYR A 34  ? 0.4472 0.3020 0.2963 -0.0783 -0.0285 0.0066  34  TYR A CA  
234  C  C   . TYR A 34  ? 0.4817 0.3346 0.3332 -0.0712 -0.0287 0.0119  34  TYR A C   
235  O  O   . TYR A 34  ? 0.4884 0.3404 0.3395 -0.0679 -0.0288 0.0122  34  TYR A O   
236  C  CB  . TYR A 34  ? 0.4414 0.3078 0.2999 -0.0793 -0.0306 0.0027  34  TYR A CB  
237  C  CG  . TYR A 34  ? 0.4145 0.2852 0.2729 -0.0861 -0.0305 -0.0025 34  TYR A CG  
238  C  CD1 . TYR A 34  ? 0.4173 0.2870 0.2711 -0.0902 -0.0298 -0.0067 34  TYR A CD1 
239  C  CD2 . TYR A 34  ? 0.4297 0.3051 0.2921 -0.0886 -0.0308 -0.0031 34  TYR A CD2 
240  C  CE1 . TYR A 34  ? 0.4240 0.2978 0.2777 -0.0968 -0.0292 -0.0114 34  TYR A CE1 
241  C  CE2 . TYR A 34  ? 0.4172 0.2964 0.2791 -0.0949 -0.0302 -0.0077 34  TYR A CE2 
242  C  CZ  . TYR A 34  ? 0.4402 0.3186 0.2979 -0.0990 -0.0293 -0.0118 34  TYR A CZ  
243  O  OH  . TYR A 34  ? 0.4468 0.3294 0.3046 -0.1054 -0.0283 -0.0162 34  TYR A OH  
244  N  N   . THR A 35  ? 0.4624 0.3149 0.3161 -0.0690 -0.0288 0.0159  35  THR A N   
245  C  CA  . THR A 35  ? 0.4471 0.2990 0.3042 -0.0626 -0.0289 0.0211  35  THR A CA  
246  C  C   . THR A 35  ? 0.4398 0.3005 0.3062 -0.0601 -0.0307 0.0202  35  THR A C   
247  O  O   . THR A 35  ? 0.4053 0.2738 0.2780 -0.0626 -0.0324 0.0173  35  THR A O   
248  C  CB  . THR A 35  ? 0.4547 0.3073 0.3144 -0.0622 -0.0294 0.0244  35  THR A CB  
249  O  OG1 . THR A 35  ? 0.4895 0.3326 0.3392 -0.0640 -0.0277 0.0254  35  THR A OG1 
250  C  CG2 . THR A 35  ? 0.4407 0.2942 0.3052 -0.0560 -0.0296 0.0298  35  THR A CG2 
251  N  N   . LEU A 36  ? 0.4266 0.2858 0.2940 -0.0547 -0.0302 0.0234  36  LEU A N   
252  C  CA  . LEU A 36  ? 0.4484 0.3149 0.3243 -0.0518 -0.0318 0.0236  36  LEU A CA  
253  C  C   . LEU A 36  ? 0.4534 0.3202 0.3338 -0.0471 -0.0315 0.0293  36  LEU A C   
254  O  O   . LEU A 36  ? 0.4684 0.3290 0.3444 -0.0442 -0.0296 0.0331  36  LEU A O   
255  C  CB  . LEU A 36  ? 0.4433 0.3077 0.3160 -0.0499 -0.0314 0.0220  36  LEU A CB  
256  C  CG  . LEU A 36  ? 0.5107 0.3777 0.3816 -0.0544 -0.0324 0.0159  36  LEU A CG  
257  C  CD1 . LEU A 36  ? 0.4981 0.3605 0.3633 -0.0522 -0.0319 0.0150  36  LEU A CD1 
258  C  CD2 . LEU A 36  ? 0.5235 0.4005 0.4031 -0.0557 -0.0349 0.0127  36  LEU A CD2 
259  N  N   . HIS A 37  ? 0.4001 0.2746 0.2896 -0.0463 -0.0333 0.0296  37  HIS A N   
260  C  CA  . HIS A 37  ? 0.3950 0.2716 0.2904 -0.0426 -0.0334 0.0346  37  HIS A CA  
261  C  C   . HIS A 37  ? 0.3831 0.2628 0.2833 -0.0390 -0.0337 0.0355  37  HIS A C   
262  O  O   . HIS A 37  ? 0.3858 0.2679 0.2864 -0.0397 -0.0347 0.0318  37  HIS A O   
263  C  CB  . HIS A 37  ? 0.3836 0.2665 0.2857 -0.0453 -0.0356 0.0341  37  HIS A CB  
264  C  CG  . HIS A 37  ? 0.3999 0.2801 0.2975 -0.0492 -0.0355 0.0330  37  HIS A CG  
265  N  ND1 . HIS A 37  ? 0.4069 0.2849 0.3041 -0.0482 -0.0353 0.0370  37  HIS A ND1 
266  C  CD2 . HIS A 37  ? 0.3895 0.2682 0.2820 -0.0540 -0.0354 0.0286  37  HIS A CD2 
267  C  CE1 . HIS A 37  ? 0.4354 0.3102 0.3271 -0.0521 -0.0351 0.0351  37  HIS A CE1 
268  N  NE2 . HIS A 37  ? 0.3972 0.2724 0.2861 -0.0558 -0.0351 0.0301  37  HIS A NE2 
269  N  N   . TRP A 38  ? 0.4104 0.2899 0.3137 -0.0348 -0.0327 0.0405  38  TRP A N   
270  C  CA  . TRP A 38  ? 0.3919 0.2743 0.3002 -0.0315 -0.0328 0.0420  38  TRP A CA  
271  C  C   . TRP A 38  ? 0.3821 0.2701 0.2992 -0.0308 -0.0339 0.0452  38  TRP A C   
272  O  O   . TRP A 38  ? 0.3866 0.2745 0.3051 -0.0308 -0.0336 0.0482  38  TRP A O   
273  C  CB  . TRP A 38  ? 0.4247 0.3014 0.3282 -0.0269 -0.0300 0.0452  38  TRP A CB  
274  C  CG  . TRP A 38  ? 0.4440 0.3149 0.3386 -0.0272 -0.0292 0.0420  38  TRP A CG  
275  C  CD1 . TRP A 38  ? 0.4795 0.3443 0.3661 -0.0290 -0.0280 0.0407  38  TRP A CD1 
276  C  CD2 . TRP A 38  ? 0.4476 0.3179 0.3401 -0.0259 -0.0294 0.0397  38  TRP A CD2 
277  N  NE1 . TRP A 38  ? 0.4793 0.3400 0.3592 -0.0291 -0.0276 0.0377  38  TRP A NE1 
278  C  CE2 . TRP A 38  ? 0.4806 0.3446 0.3639 -0.0272 -0.0286 0.0369  38  TRP A CE2 
279  C  CE3 . TRP A 38  ? 0.4251 0.2989 0.3220 -0.0238 -0.0305 0.0396  38  TRP A CE3 
280  C  CZ2 . TRP A 38  ? 0.5078 0.3698 0.3867 -0.0263 -0.0289 0.0342  38  TRP A CZ2 
281  C  CZ3 . TRP A 38  ? 0.4555 0.3268 0.3476 -0.0225 -0.0307 0.0371  38  TRP A CZ3 
282  C  CH2 . TRP A 38  ? 0.4911 0.3569 0.3746 -0.0238 -0.0300 0.0344  38  TRP A CH2 
283  N  N   . VAL A 39  ? 0.3639 0.2563 0.2866 -0.0305 -0.0354 0.0443  39  VAL A N   
284  C  CA  . VAL A 39  ? 0.3652 0.2630 0.2962 -0.0310 -0.0370 0.0462  39  VAL A CA  
285  C  C   . VAL A 39  ? 0.3560 0.2548 0.2906 -0.0276 -0.0365 0.0485  39  VAL A C   
286  O  O   . VAL A 39  ? 0.3592 0.2569 0.2914 -0.0266 -0.0367 0.0460  39  VAL A O   
287  C  CB  . VAL A 39  ? 0.3696 0.2716 0.3030 -0.0351 -0.0398 0.0416  39  VAL A CB  
288  C  CG1 . VAL A 39  ? 0.3919 0.2987 0.3334 -0.0356 -0.0417 0.0433  39  VAL A CG1 
289  C  CG2 . VAL A 39  ? 0.4050 0.3059 0.3348 -0.0388 -0.0402 0.0396  39  VAL A CG2 
290  N  N   . LYS A 40  ? 0.3645 0.2655 0.3049 -0.0261 -0.0360 0.0531  40  LYS A N   
291  C  CA  . LYS A 40  ? 0.3491 0.2512 0.2934 -0.0233 -0.0353 0.0557  40  LYS A CA  
292  C  C   . LYS A 40  ? 0.3598 0.2665 0.3109 -0.0256 -0.0380 0.0548  40  LYS A C   
293  O  O   . LYS A 40  ? 0.3550 0.2650 0.3101 -0.0283 -0.0396 0.0551  40  LYS A O   
294  C  CB  . LYS A 40  ? 0.3599 0.2621 0.3070 -0.0206 -0.0328 0.0615  40  LYS A CB  
295  C  CG  . LYS A 40  ? 0.3692 0.2720 0.3199 -0.0177 -0.0313 0.0648  40  LYS A CG  
296  C  CD  . LYS A 40  ? 0.4113 0.3149 0.3648 -0.0150 -0.0285 0.0703  40  LYS A CD  
297  C  CE  . LYS A 40  ? 0.4095 0.3145 0.3675 -0.0128 -0.0268 0.0739  40  LYS A CE  
298  N  NZ  . LYS A 40  ? 0.4367 0.3428 0.3972 -0.0099 -0.0236 0.0791  40  LYS A NZ  
299  N  N   . GLN A 41  ? 0.3485 0.2552 0.3005 -0.0246 -0.0386 0.0536  41  GLN A N   
300  C  CA  . GLN A 41  ? 0.3391 0.2493 0.2969 -0.0265 -0.0411 0.0529  41  GLN A CA  
301  C  C   . GLN A 41  ? 0.3700 0.2798 0.3311 -0.0240 -0.0397 0.0570  41  GLN A C   
302  O  O   . GLN A 41  ? 0.3849 0.2911 0.3421 -0.0208 -0.0380 0.0575  41  GLN A O   
303  C  CB  . GLN A 41  ? 0.3459 0.2557 0.3007 -0.0271 -0.0430 0.0476  41  GLN A CB  
304  C  CG  . GLN A 41  ? 0.3391 0.2512 0.2985 -0.0283 -0.0455 0.0463  41  GLN A CG  
305  C  CD  . GLN A 41  ? 0.3382 0.2505 0.2948 -0.0285 -0.0474 0.0408  41  GLN A CD  
306  O  OE1 . GLN A 41  ? 0.3755 0.2854 0.3279 -0.0260 -0.0468 0.0394  41  GLN A OE1 
307  N  NE2 . GLN A 41  ? 0.3585 0.2738 0.3174 -0.0314 -0.0498 0.0374  41  GLN A NE2 
308  N  N   . THR A 42  ? 0.3856 0.2986 0.3534 -0.0257 -0.0407 0.0595  42  THR A N   
309  C  CA  . THR A 42  ? 0.3688 0.2817 0.3405 -0.0244 -0.0398 0.0629  42  THR A CA  
310  C  C   . THR A 42  ? 0.4075 0.3227 0.3840 -0.0275 -0.0428 0.0616  42  THR A C   
311  O  O   . THR A 42  ? 0.4075 0.3252 0.3854 -0.0305 -0.0451 0.0592  42  THR A O   
312  C  CB  . THR A 42  ? 0.4104 0.3251 0.3860 -0.0232 -0.0372 0.0685  42  THR A CB  
313  O  OG1 . THR A 42  ? 0.4385 0.3573 0.4185 -0.0260 -0.0387 0.0692  42  THR A OG1 
314  C  CG2 . THR A 42  ? 0.4623 0.3742 0.4329 -0.0198 -0.0339 0.0701  42  THR A CG2 
315  N  N   . PRO A 43  ? 0.4549 0.3688 0.4334 -0.0269 -0.0428 0.0630  43  PRO A N   
316  C  CA  . PRO A 43  ? 0.4828 0.3980 0.4653 -0.0298 -0.0457 0.0618  43  PRO A CA  
317  C  C   . PRO A 43  ? 0.6209 0.5406 0.6099 -0.0332 -0.0468 0.0641  43  PRO A C   
318  O  O   . PRO A 43  ? 0.6462 0.5676 0.6368 -0.0364 -0.0497 0.0615  43  PRO A O   
319  C  CB  . PRO A 43  ? 0.5303 0.4422 0.5129 -0.0280 -0.0445 0.0640  43  PRO A CB  
320  C  CG  . PRO A 43  ? 0.4382 0.3465 0.4150 -0.0239 -0.0418 0.0646  43  PRO A CG  
321  C  CD  . PRO A 43  ? 0.4382 0.3484 0.4139 -0.0233 -0.0400 0.0655  43  PRO A CD  
322  N  N   . GLY A 44  ? 0.5454 0.4673 0.5379 -0.0325 -0.0445 0.0689  44  GLY A N   
323  C  CA  . GLY A 44  ? 0.5612 0.4878 0.5605 -0.0353 -0.0455 0.0718  44  GLY A CA  
324  C  C   . GLY A 44  ? 0.6253 0.5548 0.6246 -0.0364 -0.0464 0.0712  44  GLY A C   
325  O  O   . GLY A 44  ? 0.6988 0.6318 0.7025 -0.0394 -0.0488 0.0716  44  GLY A O   
326  N  N   . GLN A 45  ? 0.5200 0.4477 0.5142 -0.0339 -0.0446 0.0704  45  GLN A N   
327  C  CA  . GLN A 45  ? 0.4860 0.4155 0.4792 -0.0347 -0.0452 0.0701  45  GLN A CA  
328  C  C   . GLN A 45  ? 0.5150 0.4421 0.5022 -0.0361 -0.0469 0.0648  45  GLN A C   
329  O  O   . GLN A 45  ? 0.6006 0.5280 0.5856 -0.0369 -0.0473 0.0640  45  GLN A O   
330  C  CB  . GLN A 45  ? 0.5534 0.4831 0.5460 -0.0315 -0.0421 0.0740  45  GLN A CB  
331  C  CG  . GLN A 45  ? 0.5805 0.5150 0.5811 -0.0312 -0.0412 0.0793  45  GLN A CG  
332  C  CD  . GLN A 45  ? 0.6198 0.5549 0.6205 -0.0272 -0.0376 0.0834  45  GLN A CD  
333  O  OE1 . GLN A 45  ? 0.5664 0.4982 0.5609 -0.0250 -0.0361 0.0826  45  GLN A OE1 
334  N  NE2 . GLN A 45  ? 0.6697 0.6087 0.6771 -0.0265 -0.0359 0.0879  45  GLN A NE2 
335  N  N   . GLY A 46  ? 0.4357 0.3606 0.4203 -0.0363 -0.0478 0.0610  46  GLY A N   
336  C  CA  . GLY A 46  ? 0.4305 0.3543 0.4101 -0.0378 -0.0492 0.0559  46  GLY A CA  
337  C  C   . GLY A 46  ? 0.4546 0.3758 0.4281 -0.0358 -0.0470 0.0552  46  GLY A C   
338  O  O   . GLY A 46  ? 0.3969 0.3155 0.3679 -0.0326 -0.0447 0.0566  46  GLY A O   
339  N  N   . LEU A 47  ? 0.3867 0.3078 0.3571 -0.0378 -0.0476 0.0531  47  LEU A N   
340  C  CA  . LEU A 47  ? 0.3497 0.2676 0.3134 -0.0365 -0.0457 0.0518  47  LEU A CA  
341  C  C   . LEU A 47  ? 0.3854 0.3029 0.3488 -0.0358 -0.0444 0.0556  47  LEU A C   
342  O  O   . LEU A 47  ? 0.4223 0.3425 0.3895 -0.0376 -0.0460 0.0572  47  LEU A O   
343  C  CB  . LEU A 47  ? 0.3712 0.2886 0.3307 -0.0393 -0.0471 0.0463  47  LEU A CB  
344  C  CG  . LEU A 47  ? 0.3738 0.2923 0.3337 -0.0398 -0.0486 0.0420  47  LEU A CG  
345  C  CD1 . LEU A 47  ? 0.4335 0.3526 0.3898 -0.0428 -0.0497 0.0369  47  LEU A CD1 
346  C  CD2 . LEU A 47  ? 0.4045 0.3205 0.3619 -0.0363 -0.0471 0.0422  47  LEU A CD2 
347  N  N   . ASP A 48  ? 0.3853 0.2992 0.3440 -0.0329 -0.0417 0.0569  48  ASP A N   
348  C  CA  . ASP A 48  ? 0.3876 0.3001 0.3448 -0.0314 -0.0402 0.0604  48  ASP A CA  
349  C  C   . ASP A 48  ? 0.3862 0.2934 0.3346 -0.0311 -0.0387 0.0580  48  ASP A C   
350  O  O   . ASP A 48  ? 0.4117 0.3157 0.3558 -0.0294 -0.0372 0.0565  48  ASP A O   
351  C  CB  . ASP A 48  ? 0.4652 0.3783 0.4258 -0.0274 -0.0377 0.0653  48  ASP A CB  
352  C  CG  . ASP A 48  ? 0.6474 0.5641 0.6136 -0.0267 -0.0377 0.0700  48  ASP A CG  
353  O  OD1 . ASP A 48  ? 0.7863 0.7024 0.7504 -0.0277 -0.0385 0.0700  48  ASP A OD1 
354  O  OD2 . ASP A 48  ? 0.6272 0.5471 0.5994 -0.0251 -0.0368 0.0736  48  ASP A OD2 
355  N  N   . TRP A 49  ? 0.3889 0.2945 0.3341 -0.0327 -0.0391 0.0580  49  TRP A N   
356  C  CA  . TRP A 49  ? 0.3803 0.2801 0.3167 -0.0328 -0.0376 0.0559  49  TRP A CA  
357  C  C   . TRP A 49  ? 0.3934 0.2892 0.3266 -0.0283 -0.0345 0.0598  49  TRP A C   
358  O  O   . TRP A 49  ? 0.4186 0.3155 0.3546 -0.0262 -0.0340 0.0640  49  TRP A O   
359  C  CB  . TRP A 49  ? 0.3709 0.2698 0.3044 -0.0361 -0.0390 0.0548  49  TRP A CB  
360  C  CG  . TRP A 49  ? 0.3929 0.2852 0.3168 -0.0369 -0.0374 0.0525  49  TRP A CG  
361  C  CD1 . TRP A 49  ? 0.4321 0.3221 0.3507 -0.0396 -0.0373 0.0477  49  TRP A CD1 
362  C  CD2 . TRP A 49  ? 0.3927 0.2795 0.3108 -0.0350 -0.0357 0.0553  49  TRP A CD2 
363  N  NE1 . TRP A 49  ? 0.4185 0.3018 0.3284 -0.0401 -0.0357 0.0472  49  TRP A NE1 
364  C  CE2 . TRP A 49  ? 0.4264 0.3071 0.3354 -0.0371 -0.0346 0.0518  49  TRP A CE2 
365  C  CE3 . TRP A 49  ? 0.4561 0.3427 0.3759 -0.0317 -0.0351 0.0603  49  TRP A CE3 
366  C  CZ2 . TRP A 49  ? 0.4639 0.3373 0.3647 -0.0360 -0.0329 0.0532  49  TRP A CZ2 
367  C  CZ3 . TRP A 49  ? 0.4780 0.3578 0.3901 -0.0301 -0.0334 0.0617  49  TRP A CZ3 
368  C  CH2 . TRP A 49  ? 0.4575 0.3303 0.3598 -0.0323 -0.0323 0.0582  49  TRP A CH2 
369  N  N   . ILE A 50  ? 0.4155 0.3066 0.3426 -0.0266 -0.0325 0.0583  50  ILE A N   
370  C  CA  . ILE A 50  ? 0.3999 0.2864 0.3230 -0.0221 -0.0294 0.0615  50  ILE A CA  
371  C  C   . ILE A 50  ? 0.4266 0.3066 0.3414 -0.0222 -0.0282 0.0614  50  ILE A C   
372  O  O   . ILE A 50  ? 0.4217 0.2997 0.3357 -0.0189 -0.0266 0.0654  50  ILE A O   
373  C  CB  . ILE A 50  ? 0.3867 0.2704 0.3065 -0.0202 -0.0279 0.0600  50  ILE A CB  
374  C  CG1 . ILE A 50  ? 0.3742 0.2631 0.3017 -0.0190 -0.0285 0.0615  50  ILE A CG1 
375  C  CG2 . ILE A 50  ? 0.4111 0.2880 0.3238 -0.0160 -0.0245 0.0624  50  ILE A CG2 
376  C  CD1 . ILE A 50  ? 0.3788 0.2655 0.3030 -0.0179 -0.0280 0.0590  50  ILE A CD1 
377  N  N   . GLY A 51  ? 0.3969 0.2735 0.3054 -0.0258 -0.0290 0.0568  51  GLY A N   
378  C  CA  . GLY A 51  ? 0.4190 0.2882 0.3183 -0.0262 -0.0277 0.0564  51  GLY A CA  
379  C  C   . GLY A 51  ? 0.4169 0.2833 0.3101 -0.0307 -0.0284 0.0508  51  GLY A C   
380  O  O   . GLY A 51  ? 0.4312 0.3021 0.3280 -0.0327 -0.0299 0.0476  51  GLY A O   
381  N  N   . ALA A 52  ? 0.4000 0.2589 0.2839 -0.0318 -0.0271 0.0498  52  ALA A N   
382  C  CA  . ALA A 52  ? 0.4056 0.2620 0.2836 -0.0367 -0.0276 0.0445  52  ALA A CA  
383  C  C   . ALA A 52  ? 0.4546 0.3008 0.3214 -0.0358 -0.0252 0.0443  52  ALA A C   
384  O  O   . ALA A 52  ? 0.4615 0.3023 0.3245 -0.0323 -0.0235 0.0481  52  ALA A O   
385  C  CB  . ALA A 52  ? 0.4463 0.3047 0.3249 -0.0416 -0.0294 0.0426  52  ALA A CB  
386  N  N   . ILE A 53  ? 0.4175 0.2613 0.2790 -0.0392 -0.0252 0.0397  53  ILE A N   
387  C  CA  . ILE A 53  ? 0.4491 0.2827 0.2991 -0.0395 -0.0231 0.0387  53  ILE A CA  
388  C  C   . ILE A 53  ? 0.4573 0.2896 0.3026 -0.0462 -0.0238 0.0336  53  ILE A C   
389  O  O   . ILE A 53  ? 0.4664 0.3060 0.3171 -0.0496 -0.0257 0.0299  53  ILE A O   
390  C  CB  . ILE A 53  ? 0.4721 0.3031 0.3194 -0.0363 -0.0220 0.0383  53  ILE A CB  
391  C  CG1 . ILE A 53  ? 0.4856 0.3047 0.3199 -0.0362 -0.0197 0.0376  53  ILE A CG1 
392  C  CG2 . ILE A 53  ? 0.4792 0.3171 0.3312 -0.0388 -0.0240 0.0339  53  ILE A CG2 
393  C  CD1 . ILE A 53  ? 0.5020 0.3174 0.3332 -0.0314 -0.0182 0.0388  53  ILE A CD1 
394  N  N   . TYR A 54  ? 0.4722 0.2948 0.3071 -0.0479 -0.0222 0.0335  54  TYR A N   
395  C  CA  . TYR A 54  ? 0.4873 0.3073 0.3162 -0.0544 -0.0223 0.0286  54  TYR A CA  
396  C  C   . TYR A 54  ? 0.5039 0.3178 0.3253 -0.0547 -0.0211 0.0262  54  TYR A C   
397  O  O   . TYR A 54  ? 0.5460 0.3497 0.3585 -0.0520 -0.0191 0.0285  54  TYR A O   
398  C  CB  . TYR A 54  ? 0.4752 0.2875 0.2964 -0.0570 -0.0212 0.0296  54  TYR A CB  
399  C  CG  . TYR A 54  ? 0.4842 0.2946 0.2999 -0.0645 -0.0211 0.0245  54  TYR A CG  
400  C  CD1 . TYR A 54  ? 0.4825 0.3025 0.3053 -0.0691 -0.0228 0.0207  54  TYR A CD1 
401  C  CD2 . TYR A 54  ? 0.5198 0.3191 0.3234 -0.0668 -0.0192 0.0231  54  TYR A CD2 
402  C  CE1 . TYR A 54  ? 0.5094 0.3286 0.3279 -0.0761 -0.0225 0.0160  54  TYR A CE1 
403  C  CE2 . TYR A 54  ? 0.5439 0.3422 0.3431 -0.0741 -0.0190 0.0183  54  TYR A CE2 
404  C  CZ  . TYR A 54  ? 0.5235 0.3318 0.3302 -0.0787 -0.0205 0.0149  54  TYR A CZ  
405  O  OH  . TYR A 54  ? 0.5731 0.3807 0.3755 -0.0860 -0.0199 0.0101  54  TYR A OH  
406  N  N   . PRO A 55  ? 0.4909 0.3104 0.3153 -0.0573 -0.0225 0.0218  55  PRO A N   
407  C  CA  . PRO A 55  ? 0.5017 0.3158 0.3195 -0.0565 -0.0218 0.0200  55  PRO A CA  
408  C  C   . PRO A 55  ? 0.5758 0.3784 0.3807 -0.0601 -0.0200 0.0182  55  PRO A C   
409  O  O   . PRO A 55  ? 0.5906 0.3851 0.3876 -0.0581 -0.0188 0.0185  55  PRO A O   
410  C  CB  . PRO A 55  ? 0.4978 0.3221 0.3227 -0.0592 -0.0242 0.0153  55  PRO A CB  
411  C  CG  . PRO A 55  ? 0.4607 0.2955 0.2975 -0.0579 -0.0258 0.0167  55  PRO A CG  
412  C  CD  . PRO A 55  ? 0.4683 0.2997 0.3029 -0.0598 -0.0249 0.0188  55  PRO A CD  
413  N  N   . GLY A 56  ? 0.5614 0.3628 0.3638 -0.0657 -0.0198 0.0164  56  GLY A N   
414  C  CA  . GLY A 56  ? 0.6179 0.4083 0.4079 -0.0701 -0.0181 0.0145  56  GLY A CA  
415  C  C   . GLY A 56  ? 0.6826 0.4597 0.4623 -0.0653 -0.0158 0.0187  56  GLY A C   
416  O  O   . GLY A 56  ? 0.6540 0.4211 0.4230 -0.0670 -0.0145 0.0171  56  GLY A O   
417  N  N   . ASN A 57  ? 0.6683 0.4451 0.4510 -0.0595 -0.0152 0.0239  57  ASN A N   
418  C  CA  . ASN A 57  ? 0.6740 0.4386 0.4472 -0.0546 -0.0129 0.0280  57  ASN A CA  
419  C  C   . ASN A 57  ? 0.6660 0.4340 0.4454 -0.0465 -0.0126 0.0326  57  ASN A C   
420  O  O   . ASN A 57  ? 0.6547 0.4141 0.4278 -0.0413 -0.0105 0.0363  57  ASN A O   
421  C  CB  . ASN A 57  ? 0.6700 0.4279 0.4375 -0.0561 -0.0120 0.0300  57  ASN A CB  
422  C  CG  . ASN A 57  ? 0.6713 0.4384 0.4490 -0.0548 -0.0135 0.0326  57  ASN A CG  
423  O  OD1 . ASN A 57  ? 0.6318 0.4091 0.4206 -0.0514 -0.0148 0.0340  57  ASN A OD1 
424  N  ND2 . ASN A 57  ? 0.6562 0.4192 0.4297 -0.0574 -0.0133 0.0334  57  ASN A ND2 
425  N  N   . GLY A 58  ? 0.5767 0.3571 0.3684 -0.0452 -0.0144 0.0325  58  GLY A N   
426  C  CA  . GLY A 58  ? 0.5849 0.3681 0.3820 -0.0380 -0.0138 0.0368  58  GLY A CA  
427  C  C   . GLY A 58  ? 0.5835 0.3695 0.3863 -0.0338 -0.0135 0.0419  58  GLY A C   
428  O  O   . GLY A 58  ? 0.5696 0.3581 0.3771 -0.0279 -0.0127 0.0458  58  GLY A O   
429  N  N   . ASP A 59  ? 0.5778 0.3641 0.3807 -0.0370 -0.0143 0.0420  59  ASP A N   
430  C  CA  . ASP A 59  ? 0.5702 0.3599 0.3788 -0.0337 -0.0147 0.0465  59  ASP A CA  
431  C  C   . ASP A 59  ? 0.5417 0.3447 0.3644 -0.0323 -0.0167 0.0475  59  ASP A C   
432  O  O   . ASP A 59  ? 0.5533 0.3633 0.3813 -0.0364 -0.0185 0.0438  59  ASP A O   
433  C  CB  . ASP A 59  ? 0.5623 0.3501 0.3678 -0.0386 -0.0157 0.0455  59  ASP A CB  
434  C  CG  . ASP A 59  ? 0.6563 0.4302 0.4479 -0.0390 -0.0138 0.0460  59  ASP A CG  
435  O  OD1 . ASP A 59  ? 0.6642 0.4295 0.4481 -0.0354 -0.0116 0.0471  59  ASP A OD1 
436  O  OD2 . ASP A 59  ? 0.6662 0.4377 0.4545 -0.0428 -0.0144 0.0454  59  ASP A OD2 
437  N  N   . THR A 60  ? 0.5475 0.3539 0.3763 -0.0267 -0.0163 0.0525  60  THR A N   
438  C  CA  . THR A 60  ? 0.5180 0.3362 0.3598 -0.0253 -0.0179 0.0537  60  THR A CA  
439  C  C   . THR A 60  ? 0.5471 0.3702 0.3955 -0.0238 -0.0191 0.0575  60  THR A C   
440  O  O   . THR A 60  ? 0.5671 0.3841 0.4103 -0.0213 -0.0180 0.0604  60  THR A O   
441  C  CB  . THR A 60  ? 0.5490 0.3674 0.3925 -0.0198 -0.0160 0.0560  60  THR A CB  
442  O  OG1 . THR A 60  ? 0.5831 0.3938 0.4204 -0.0146 -0.0134 0.0599  60  THR A OG1 
443  C  CG2 . THR A 60  ? 0.5232 0.3388 0.3619 -0.0214 -0.0156 0.0521  60  THR A CG2 
444  N  N   . SER A 61  ? 0.4871 0.3206 0.3465 -0.0253 -0.0214 0.0573  61  SER A N   
445  C  CA  . SER A 61  ? 0.4872 0.3273 0.3551 -0.0233 -0.0228 0.0613  61  SER A CA  
446  C  C   . SER A 61  ? 0.4779 0.3271 0.3567 -0.0212 -0.0234 0.0627  61  SER A C   
447  O  O   . SER A 61  ? 0.4787 0.3311 0.3599 -0.0236 -0.0241 0.0594  61  SER A O   
448  C  CB  . SER A 61  ? 0.5550 0.3983 0.4249 -0.0281 -0.0255 0.0595  61  SER A CB  
449  O  OG  . SER A 61  ? 0.7197 0.5540 0.5789 -0.0302 -0.0248 0.0584  61  SER A OG  
450  N  N   . TYR A 62  ? 0.4970 0.3499 0.3820 -0.0168 -0.0229 0.0675  62  TYR A N   
451  C  CA  . TYR A 62  ? 0.4868 0.3478 0.3819 -0.0147 -0.0230 0.0694  62  TYR A CA  
452  C  C   . TYR A 62  ? 0.4842 0.3535 0.3892 -0.0150 -0.0253 0.0721  62  TYR A C   
453  O  O   . TYR A 62  ? 0.4900 0.3585 0.3944 -0.0139 -0.0259 0.0746  62  TYR A O   
454  C  CB  . TYR A 62  ? 0.4840 0.3429 0.3786 -0.0086 -0.0197 0.0732  62  TYR A CB  
455  C  CG  . TYR A 62  ? 0.5021 0.3528 0.3871 -0.0076 -0.0174 0.0709  62  TYR A CG  
456  C  CD1 . TYR A 62  ? 0.5413 0.3819 0.4149 -0.0067 -0.0157 0.0703  62  TYR A CD1 
457  C  CD2 . TYR A 62  ? 0.5149 0.3677 0.4019 -0.0077 -0.0171 0.0691  62  TYR A CD2 
458  C  CE1 . TYR A 62  ? 0.5807 0.4137 0.4454 -0.0061 -0.0137 0.0681  62  TYR A CE1 
459  C  CE2 . TYR A 62  ? 0.5327 0.3782 0.4109 -0.0068 -0.0152 0.0670  62  TYR A CE2 
460  C  CZ  . TYR A 62  ? 0.5203 0.3560 0.3875 -0.0062 -0.0136 0.0663  62  TYR A CZ  
461  O  OH  . TYR A 62  ? 0.5422 0.3705 0.4004 -0.0058 -0.0121 0.0639  62  TYR A OH  
462  N  N   . ASN A 63  ? 0.4535 0.3305 0.3674 -0.0167 -0.0269 0.0715  63  ASN A N   
463  C  CA  . ASN A 63  ? 0.4734 0.3588 0.3978 -0.0163 -0.0287 0.0747  63  ASN A CA  
464  C  C   . ASN A 63  ? 0.4778 0.3642 0.4051 -0.0105 -0.0261 0.0799  63  ASN A C   
465  O  O   . ASN A 63  ? 0.4841 0.3678 0.4092 -0.0074 -0.0232 0.0806  63  ASN A O   
466  C  CB  . ASN A 63  ? 0.4602 0.3517 0.3918 -0.0188 -0.0302 0.0729  63  ASN A CB  
467  C  CG  . ASN A 63  ? 0.5042 0.4040 0.4462 -0.0198 -0.0326 0.0752  63  ASN A CG  
468  O  OD1 . ASN A 63  ? 0.4993 0.4019 0.4454 -0.0172 -0.0324 0.0794  63  ASN A OD1 
469  N  ND2 . ASN A 63  ? 0.4378 0.3417 0.3844 -0.0234 -0.0349 0.0725  63  ASN A ND2 
470  N  N   . GLN A 64  ? 0.4666 0.3562 0.3979 -0.0089 -0.0271 0.0834  64  GLN A N   
471  C  CA  . GLN A 64  ? 0.5365 0.4280 0.4713 -0.0032 -0.0246 0.0885  64  GLN A CA  
472  C  C   . GLN A 64  ? 0.5247 0.4214 0.4667 -0.0016 -0.0228 0.0900  64  GLN A C   
473  O  O   . GLN A 64  ? 0.5067 0.4015 0.4475 0.0030  -0.0193 0.0925  64  GLN A O   
474  C  CB  . GLN A 64  ? 0.5763 0.4735 0.5173 -0.0026 -0.0269 0.0917  64  GLN A CB  
475  C  CG  . GLN A 64  ? 0.7376 0.6385 0.6836 0.0034  -0.0246 0.0970  64  GLN A CG  
476  N  N   . LYS A 65  ? 0.5201 0.4225 0.4689 -0.0054 -0.0251 0.0884  65  LYS A N   
477  C  CA  . LYS A 65  ? 0.5269 0.4339 0.4824 -0.0041 -0.0235 0.0902  65  LYS A CA  
478  C  C   . LYS A 65  ? 0.5210 0.4216 0.4695 -0.0023 -0.0205 0.0885  65  LYS A C   
479  O  O   . LYS A 65  ? 0.5459 0.4487 0.4981 0.0002  -0.0181 0.0908  65  LYS A O   
480  C  CB  . LYS A 65  ? 0.5299 0.4439 0.4940 -0.0085 -0.0267 0.0891  65  LYS A CB  
481  C  CG  . LYS A 65  ? 0.5658 0.4772 0.5260 -0.0130 -0.0290 0.0839  65  LYS A CG  
482  C  CD  . LYS A 65  ? 0.6470 0.5651 0.6157 -0.0168 -0.0321 0.0833  65  LYS A CD  
483  C  CE  . LYS A 65  ? 0.5777 0.4996 0.5530 -0.0148 -0.0302 0.0863  65  LYS A CE  
484  N  NZ  . LYS A 65  ? 0.6134 0.5385 0.5935 -0.0185 -0.0326 0.0843  65  LYS A NZ  
485  N  N   . PHE A 66  ? 0.4897 0.3827 0.4282 -0.0035 -0.0205 0.0846  66  PHE A N   
486  C  CA  . PHE A 66  ? 0.4721 0.3593 0.4038 -0.0021 -0.0182 0.0826  66  PHE A CA  
487  C  C   . PHE A 66  ? 0.4982 0.3768 0.4198 0.0014  -0.0153 0.0832  66  PHE A C   
488  O  O   . PHE A 66  ? 0.5300 0.4025 0.4443 0.0023  -0.0136 0.0811  66  PHE A O   
489  C  CB  . PHE A 66  ? 0.4691 0.3543 0.3969 -0.0068 -0.0207 0.0770  66  PHE A CB  
490  C  CG  . PHE A 66  ? 0.4505 0.3427 0.3869 -0.0096 -0.0230 0.0762  66  PHE A CG  
491  C  CD1 . PHE A 66  ? 0.4639 0.3572 0.4028 -0.0080 -0.0218 0.0769  66  PHE A CD1 
492  C  CD2 . PHE A 66  ? 0.4290 0.3259 0.3704 -0.0137 -0.0265 0.0748  66  PHE A CD2 
493  C  CE1 . PHE A 66  ? 0.4322 0.3310 0.3783 -0.0105 -0.0239 0.0762  66  PHE A CE1 
494  C  CE2 . PHE A 66  ? 0.4416 0.3442 0.3904 -0.0162 -0.0286 0.0740  66  PHE A CE2 
495  C  CZ  . PHE A 66  ? 0.4766 0.3799 0.4276 -0.0145 -0.0273 0.0747  66  PHE A CZ  
496  N  N   . LYS A 67  ? 0.4905 0.3681 0.4113 0.0038  -0.0146 0.0860  67  LYS A N   
497  C  CA  . LYS A 67  ? 0.5654 0.4336 0.4753 0.0068  -0.0121 0.0860  67  LYS A CA  
498  C  C   . LYS A 67  ? 0.5852 0.4493 0.4914 0.0118  -0.0080 0.0878  67  LYS A C   
499  O  O   . LYS A 67  ? 0.7103 0.5654 0.6059 0.0129  -0.0063 0.0859  67  LYS A O   
500  C  CB  . LYS A 67  ? 0.6026 0.4694 0.5110 0.0089  -0.0123 0.0886  67  LYS A CB  
501  C  CG  . LYS A 67  ? 0.6952 0.5695 0.6131 0.0131  -0.0113 0.0939  67  LYS A CG  
502  N  N   . ASP A 68  ? 0.5738 0.4446 0.4885 0.0146  -0.0064 0.0914  68  ASP A N   
503  C  CA  . ASP A 68  ? 0.6341 0.5010 0.5451 0.0195  -0.0021 0.0934  68  ASP A CA  
504  C  C   . ASP A 68  ? 0.6042 0.4696 0.5132 0.0176  -0.0023 0.0904  68  ASP A C   
505  O  O   . ASP A 68  ? 0.6641 0.5226 0.5652 0.0203  0.0003  0.0899  68  ASP A O   
506  C  CB  . ASP A 68  ? 0.7269 0.6009 0.6470 0.0239  0.0003  0.0989  68  ASP A CB  
507  C  CG  . ASP A 68  ? 0.8573 0.7333 0.7797 0.0266  0.0003  0.1020  68  ASP A CG  
508  O  OD1 . ASP A 68  ? 0.8079 0.6754 0.7204 0.0289  0.0014  0.1014  68  ASP A OD1 
509  O  OD2 . ASP A 68  ? 0.8775 0.7633 0.8111 0.0263  -0.0009 0.1049  68  ASP A OD2 
510  N  N   . LYS A 69  ? 0.5165 0.3876 0.4317 0.0129  -0.0056 0.0882  69  LYS A N   
511  C  CA  . LYS A 69  ? 0.4738 0.3448 0.3887 0.0115  -0.0060 0.0859  69  LYS A CA  
512  C  C   . LYS A 69  ? 0.4817 0.3455 0.3867 0.0090  -0.0074 0.0807  69  LYS A C   
513  O  O   . LYS A 69  ? 0.5231 0.3832 0.4235 0.0102  -0.0063 0.0793  69  LYS A O   
514  C  CB  . LYS A 69  ? 0.4682 0.3482 0.3940 0.0078  -0.0090 0.0859  69  LYS A CB  
515  C  CG  . LYS A 69  ? 0.4678 0.3481 0.3939 0.0056  -0.0104 0.0830  69  LYS A CG  
516  C  CD  . LYS A 69  ? 0.4581 0.3365 0.3831 0.0099  -0.0067 0.0858  69  LYS A CD  
517  C  CE  . LYS A 69  ? 0.4805 0.3652 0.4146 0.0122  -0.0044 0.0912  69  LYS A CE  
518  N  NZ  . LYS A 69  ? 0.4943 0.3771 0.4272 0.0157  -0.0008 0.0937  69  LYS A NZ  
519  N  N   . ALA A 70  ? 0.4606 0.3227 0.3624 0.0054  -0.0098 0.0777  70  ALA A N   
520  C  CA  . ALA A 70  ? 0.4818 0.3391 0.3761 0.0019  -0.0117 0.0723  70  ALA A CA  
521  C  C   . ALA A 70  ? 0.5014 0.3495 0.3846 0.0027  -0.0102 0.0712  70  ALA A C   
522  O  O   . ALA A 70  ? 0.5383 0.3851 0.4210 0.0038  -0.0095 0.0735  70  ALA A O   
523  C  CB  . ALA A 70  ? 0.4696 0.3324 0.3689 -0.0036 -0.0156 0.0691  70  ALA A CB  
524  N  N   . THR A 71  ? 0.5083 0.3499 0.3827 0.0016  -0.0101 0.0675  71  THR A N   
525  C  CA  . THR A 71  ? 0.5224 0.3549 0.3858 0.0008  -0.0094 0.0654  71  THR A CA  
526  C  C   . THR A 71  ? 0.5073 0.3391 0.3671 -0.0046 -0.0121 0.0596  71  THR A C   
527  O  O   . THR A 71  ? 0.4854 0.3183 0.3452 -0.0048 -0.0129 0.0573  71  THR A O   
528  C  CB  . THR A 71  ? 0.5358 0.3593 0.3899 0.0057  -0.0058 0.0670  71  THR A CB  
529  O  OG1 . THR A 71  ? 0.5885 0.4140 0.4470 0.0111  -0.0030 0.0724  71  THR A OG1 
530  C  CG2 . THR A 71  ? 0.5331 0.3462 0.3751 0.0047  -0.0050 0.0649  71  THR A CG2 
531  N  N   . LEU A 72  ? 0.5064 0.3365 0.3633 -0.0087 -0.0136 0.0572  72  LEU A N   
532  C  CA  . LEU A 72  ? 0.4873 0.3178 0.3418 -0.0144 -0.0160 0.0516  72  LEU A CA  
533  C  C   . LEU A 72  ? 0.5133 0.3333 0.3551 -0.0155 -0.0148 0.0490  72  LEU A C   
534  O  O   . LEU A 72  ? 0.5495 0.3627 0.3851 -0.0144 -0.0130 0.0508  72  LEU A O   
535  C  CB  . LEU A 72  ? 0.4789 0.3147 0.3386 -0.0189 -0.0184 0.0504  72  LEU A CB  
536  C  CG  . LEU A 72  ? 0.4913 0.3371 0.3631 -0.0186 -0.0200 0.0526  72  LEU A CG  
537  C  CD1 . LEU A 72  ? 0.4816 0.3315 0.3566 -0.0238 -0.0225 0.0503  72  LEU A CD1 
538  C  CD2 . LEU A 72  ? 0.4845 0.3356 0.3617 -0.0177 -0.0210 0.0515  72  LEU A CD2 
539  N  N   . THR A 73  ? 0.4855 0.3045 0.3236 -0.0179 -0.0159 0.0447  73  THR A N   
540  C  CA  . THR A 73  ? 0.5404 0.3502 0.3669 -0.0202 -0.0152 0.0415  73  THR A CA  
541  C  C   . THR A 73  ? 0.5321 0.3458 0.3591 -0.0263 -0.0180 0.0356  73  THR A C   
542  O  O   . THR A 73  ? 0.5273 0.3504 0.3631 -0.0277 -0.0204 0.0340  73  THR A O   
543  C  CB  . THR A 73  ? 0.5971 0.3988 0.4155 -0.0155 -0.0129 0.0427  73  THR A CB  
544  O  OG1 . THR A 73  ? 0.5718 0.3787 0.3945 -0.0142 -0.0141 0.0416  73  THR A OG1 
545  C  CG2 . THR A 73  ? 0.5714 0.3692 0.3888 -0.0094 -0.0097 0.0484  73  THR A CG2 
546  N  N   . ALA A 74  ? 0.5232 0.3296 0.3406 -0.0298 -0.0178 0.0323  74  ALA A N   
547  C  CA  . ALA A 74  ? 0.5438 0.3537 0.3612 -0.0359 -0.0201 0.0265  74  ALA A CA  
548  C  C   . ALA A 74  ? 0.6437 0.4447 0.4497 -0.0372 -0.0195 0.0236  74  ALA A C   
549  O  O   . ALA A 74  ? 0.6267 0.4170 0.4231 -0.0359 -0.0171 0.0253  74  ALA A O   
550  C  CB  . ALA A 74  ? 0.5367 0.3481 0.3550 -0.0412 -0.0207 0.0251  74  ALA A CB  
551  N  N   . ASP A 75  ? 0.5706 0.3761 0.3779 -0.0397 -0.0218 0.0191  75  ASP A N   
552  C  CA  . ASP A 75  ? 0.6335 0.4321 0.4310 -0.0415 -0.0220 0.0156  75  ASP A CA  
553  C  C   . ASP A 75  ? 0.5704 0.3735 0.3687 -0.0490 -0.0242 0.0098  75  ASP A C   
554  O  O   . ASP A 75  ? 0.5727 0.3855 0.3781 -0.0508 -0.0269 0.0064  75  ASP A O   
555  C  CB  . ASP A 75  ? 0.6610 0.4601 0.4584 -0.0369 -0.0227 0.0159  75  ASP A CB  
556  C  CG  . ASP A 75  ? 0.7188 0.5107 0.5059 -0.0381 -0.0232 0.0125  75  ASP A CG  
557  O  OD1 . ASP A 75  ? 0.6996 0.4867 0.4800 -0.0433 -0.0232 0.0093  75  ASP A OD1 
558  O  OD2 . ASP A 75  ? 0.8066 0.5979 0.5925 -0.0340 -0.0237 0.0129  75  ASP A OD2 
559  N  N   . LYS A 76  ? 0.6300 0.4263 0.4212 -0.0535 -0.0228 0.0088  76  LYS A N   
560  C  CA  . LYS A 76  ? 0.6493 0.4492 0.4405 -0.0612 -0.0242 0.0035  76  LYS A CA  
561  C  C   . LYS A 76  ? 0.6379 0.4396 0.4268 -0.0636 -0.0264 -0.0013 76  LYS A C   
562  O  O   . LYS A 76  ? 0.6921 0.5030 0.4868 -0.0684 -0.0286 -0.0058 76  LYS A O   
563  C  CB  . LYS A 76  ? 0.6442 0.4346 0.4264 -0.0655 -0.0221 0.0035  76  LYS A CB  
564  C  CG  . LYS A 76  ? 0.6622 0.4550 0.4494 -0.0651 -0.0211 0.0068  76  LYS A CG  
565  C  CD  . LYS A 76  ? 0.7483 0.5322 0.5269 -0.0698 -0.0192 0.0067  76  LYS A CD  
566  C  CE  . LYS A 76  ? 0.7468 0.5159 0.5131 -0.0663 -0.0166 0.0100  76  LYS A CE  
567  N  NZ  . LYS A 76  ? 0.7773 0.5382 0.5355 -0.0711 -0.0150 0.0096  76  LYS A NZ  
568  N  N   . SER A 77  ? 0.6760 0.4696 0.4570 -0.0600 -0.0259 -0.0006 77  SER A N   
569  C  CA  . SER A 77  ? 0.6711 0.4656 0.4488 -0.0623 -0.0282 -0.0053 77  SER A CA  
570  C  C   . SER A 77  ? 0.6937 0.5014 0.4824 -0.0608 -0.0315 -0.0073 77  SER A C   
571  O  O   . SER A 77  ? 0.7282 0.5412 0.5180 -0.0646 -0.0341 -0.0123 77  SER A O   
572  C  CB  . SER A 77  ? 0.7613 0.5432 0.5270 -0.0587 -0.0269 -0.0040 77  SER A CB  
573  O  OG  . SER A 77  ? 0.7749 0.5559 0.5424 -0.0508 -0.0260 0.0006  77  SER A OG  
574  N  N   . SER A 78  ? 0.5995 0.4128 0.3967 -0.0556 -0.0314 -0.0036 78  SER A N   
575  C  CA  . SER A 78  ? 0.5847 0.4096 0.3918 -0.0539 -0.0344 -0.0052 78  SER A CA  
576  C  C   . SER A 78  ? 0.5412 0.3766 0.3598 -0.0554 -0.0350 -0.0049 78  SER A C   
577  O  O   . SER A 78  ? 0.5565 0.4014 0.3841 -0.0534 -0.0373 -0.0057 78  SER A O   
578  C  CB  . SER A 78  ? 0.5965 0.4187 0.4031 -0.0464 -0.0340 -0.0013 78  SER A CB  
579  O  OG  . SER A 78  ? 0.5994 0.4191 0.4082 -0.0427 -0.0313 0.0042  78  SER A OG  
580  N  N   . SER A 79  ? 0.5378 0.3710 0.3558 -0.0587 -0.0330 -0.0038 79  SER A N   
581  C  CA  . SER A 79  ? 0.5133 0.3556 0.3413 -0.0602 -0.0335 -0.0036 79  SER A CA  
582  C  C   . SER A 79  ? 0.4966 0.3430 0.3321 -0.0540 -0.0338 0.0005  79  SER A C   
583  O  O   . SER A 79  ? 0.4895 0.3457 0.3346 -0.0543 -0.0356 -0.0004 79  SER A O   
584  C  CB  . SER A 79  ? 0.5589 0.4119 0.3933 -0.0654 -0.0361 -0.0093 79  SER A CB  
585  O  OG  . SER A 79  ? 0.5953 0.4453 0.4234 -0.0718 -0.0357 -0.0133 79  SER A OG  
586  N  N   . THR A 80  ? 0.4830 0.3217 0.3140 -0.0486 -0.0318 0.0053  80  THR A N   
587  C  CA  . THR A 80  ? 0.4793 0.3216 0.3171 -0.0429 -0.0319 0.0093  80  THR A CA  
588  C  C   . THR A 80  ? 0.4881 0.3256 0.3254 -0.0401 -0.0291 0.0149  80  THR A C   
589  O  O   . THR A 80  ? 0.5043 0.3321 0.3329 -0.0391 -0.0267 0.0169  80  THR A O   
590  C  CB  . THR A 80  ? 0.5200 0.3594 0.3543 -0.0383 -0.0324 0.0098  80  THR A CB  
591  O  OG1 . THR A 80  ? 0.4872 0.3326 0.3233 -0.0406 -0.0355 0.0046  80  THR A OG1 
592  C  CG2 . THR A 80  ? 0.4820 0.3246 0.3227 -0.0326 -0.0322 0.0140  80  THR A CG2 
593  N  N   . ALA A 81  ? 0.4541 0.2982 0.3006 -0.0385 -0.0295 0.0175  81  ALA A N   
594  C  CA  . ALA A 81  ? 0.4790 0.3201 0.3265 -0.0352 -0.0273 0.0231  81  ALA A CA  
595  C  C   . ALA A 81  ? 0.4564 0.2983 0.3072 -0.0292 -0.0267 0.0268  81  ALA A C   
596  O  O   . ALA A 81  ? 0.4801 0.3274 0.3354 -0.0283 -0.0286 0.0252  81  ALA A O   
597  C  CB  . ALA A 81  ? 0.4920 0.3398 0.3475 -0.0377 -0.0282 0.0237  81  ALA A CB  
598  N  N   . TYR A 82  ? 0.4485 0.2853 0.2973 -0.0252 -0.0240 0.0319  82  TYR A N   
599  C  CA  . TYR A 82  ? 0.4905 0.3278 0.3421 -0.0196 -0.0229 0.0357  82  TYR A CA  
600  C  C   . TYR A 82  ? 0.4758 0.3148 0.3329 -0.0169 -0.0211 0.0410  82  TYR A C   
601  O  O   . TYR A 82  ? 0.4714 0.3075 0.3264 -0.0177 -0.0199 0.0426  82  TYR A O   
602  C  CB  . TYR A 82  ? 0.5228 0.3504 0.3643 -0.0159 -0.0203 0.0371  82  TYR A CB  
603  C  CG  . TYR A 82  ? 0.5513 0.3755 0.3857 -0.0175 -0.0217 0.0325  82  TYR A CG  
604  C  CD1 . TYR A 82  ? 0.5274 0.3550 0.3640 -0.0156 -0.0233 0.0313  82  TYR A CD1 
605  C  CD2 . TYR A 82  ? 0.5466 0.3650 0.3725 -0.0214 -0.0218 0.0290  82  TYR A CD2 
606  C  CE1 . TYR A 82  ? 0.5930 0.4183 0.4236 -0.0170 -0.0250 0.0270  82  TYR A CE1 
607  C  CE2 . TYR A 82  ? 0.5903 0.4070 0.4108 -0.0234 -0.0235 0.0244  82  TYR A CE2 
608  C  CZ  . TYR A 82  ? 0.6346 0.4548 0.4574 -0.0210 -0.0253 0.0235  82  TYR A CZ  
609  O  OH  . TYR A 82  ? 0.6287 0.4476 0.4464 -0.0224 -0.0273 0.0191  82  TYR A OH  
610  N  N   . MET A 83  ? 0.4405 0.2844 0.3048 -0.0138 -0.0211 0.0438  83  MET A N   
611  C  CA  . MET A 83  ? 0.4549 0.3007 0.3246 -0.0108 -0.0193 0.0492  83  MET A CA  
612  C  C   . MET A 83  ? 0.4841 0.3277 0.3532 -0.0054 -0.0169 0.0527  83  MET A C   
613  O  O   . MET A 83  ? 0.4843 0.3303 0.3555 -0.0044 -0.0179 0.0519  83  MET A O   
614  C  CB  . MET A 83  ? 0.4445 0.2996 0.3253 -0.0130 -0.0216 0.0496  83  MET A CB  
615  C  CG  . MET A 83  ? 0.4228 0.2807 0.3100 -0.0100 -0.0200 0.0551  83  MET A CG  
616  S  SD  . MET A 83  ? 0.4754 0.3430 0.3744 -0.0132 -0.0228 0.0556  83  MET A SD  
617  C  CE  . MET A 83  ? 0.4874 0.3593 0.3908 -0.0132 -0.0248 0.0534  83  MET A CE  
618  N  N   . GLN A 84  ? 0.4799 0.3189 0.3459 -0.0016 -0.0136 0.0569  84  GLN A N   
619  C  CA  . GLN A 84  ? 0.4728 0.3105 0.3392 0.0035  -0.0108 0.0608  84  GLN A CA  
620  C  C   . GLN A 84  ? 0.4888 0.3337 0.3658 0.0049  -0.0101 0.0654  84  GLN A C   
621  O  O   . GLN A 84  ? 0.4837 0.3304 0.3637 0.0043  -0.0099 0.0672  84  GLN A O   
622  C  CB  . GLN A 84  ? 0.5025 0.3311 0.3593 0.0072  -0.0073 0.0627  84  GLN A CB  
623  C  CG  . GLN A 84  ? 0.5802 0.4064 0.4358 0.0129  -0.0039 0.0666  84  GLN A CG  
624  C  CD  . GLN A 84  ? 0.7555 0.5753 0.6055 0.0175  0.0002  0.0702  84  GLN A CD  
625  O  OE1 . GLN A 84  ? 0.8099 0.6320 0.6640 0.0184  0.0012  0.0732  84  GLN A OE1 
626  N  NE2 . GLN A 84  ? 0.7655 0.5772 0.6060 0.0209  0.0026  0.0702  84  GLN A NE2 
627  N  N   . LEU A 85  ? 0.4692 0.3178 0.3514 0.0069  -0.0097 0.0673  85  LEU A N   
628  C  CA  . LEU A 85  ? 0.4910 0.3458 0.3828 0.0086  -0.0084 0.0721  85  LEU A CA  
629  C  C   . LEU A 85  ? 0.5027 0.3536 0.3914 0.0141  -0.0039 0.0763  85  LEU A C   
630  O  O   . LEU A 85  ? 0.5337 0.3806 0.4173 0.0160  -0.0030 0.0755  85  LEU A O   
631  C  CB  . LEU A 85  ? 0.4737 0.3352 0.3735 0.0062  -0.0110 0.0712  85  LEU A CB  
632  C  CG  . LEU A 85  ? 0.4820 0.3475 0.3847 0.0010  -0.0152 0.0669  85  LEU A CG  
633  C  CD1 . LEU A 85  ? 0.4439 0.3142 0.3528 0.0000  -0.0172 0.0663  85  LEU A CD1 
634  C  CD2 . LEU A 85  ? 0.4668 0.3368 0.3753 -0.0013 -0.0163 0.0682  85  LEU A CD2 
635  N  N   . SER A 86  ? 0.4989 0.3510 0.3904 0.0168  -0.0012 0.0805  86  SER A N   
636  C  CA  . SER A 86  ? 0.5244 0.3727 0.4125 0.0224  0.0033  0.0844  86  SER A CA  
637  C  C   . SER A 86  ? 0.5126 0.3685 0.4113 0.0241  0.0051  0.0891  86  SER A C   
638  O  O   . SER A 86  ? 0.5263 0.3901 0.4347 0.0209  0.0027  0.0896  86  SER A O   
639  C  CB  . SER A 86  ? 0.5516 0.3947 0.4339 0.0249  0.0055  0.0856  86  SER A CB  
640  O  OG  . SER A 86  ? 0.5915 0.4413 0.4824 0.0241  0.0047  0.0880  86  SER A OG  
641  N  N   . ASN A 87  ? 0.5221 0.3755 0.4186 0.0287  0.0094  0.0924  87  ASN A N   
642  C  CA  . ASN A 87  ? 0.5048 0.3650 0.4108 0.0304  0.0119  0.0971  87  ASN A CA  
643  C  C   . ASN A 87  ? 0.4913 0.3584 0.4061 0.0261  0.0087  0.0964  87  ASN A C   
644  O  O   . ASN A 87  ? 0.4932 0.3684 0.4184 0.0244  0.0079  0.0987  87  ASN A O   
645  C  CB  . ASN A 87  ? 0.5684 0.4341 0.4813 0.0320  0.0134  0.1009  87  ASN A CB  
646  C  CG  . ASN A 87  ? 0.6577 0.5161 0.5616 0.0368  0.0169  0.1019  87  ASN A CG  
647  O  OD1 . ASN A 87  ? 0.6891 0.5420 0.5866 0.0409  0.0207  0.1032  87  ASN A OD1 
648  N  ND2 . ASN A 87  ? 0.6356 0.4927 0.5376 0.0364  0.0154  0.1010  87  ASN A ND2 
649  N  N   . LEU A 88  ? 0.4942 0.3578 0.4045 0.0247  0.0068  0.0932  88  LEU A N   
650  C  CA  . LEU A 88  ? 0.4937 0.3625 0.4108 0.0206  0.0032  0.0917  88  LEU A CA  
651  C  C   . LEU A 88  ? 0.5106 0.3856 0.4372 0.0210  0.0053  0.0963  88  LEU A C   
652  O  O   . LEU A 88  ? 0.5337 0.4069 0.4588 0.0247  0.0096  0.0997  88  LEU A O   
653  C  CB  . LEU A 88  ? 0.4887 0.3517 0.3979 0.0202  0.0015  0.0877  88  LEU A CB  
654  C  CG  . LEU A 88  ? 0.5272 0.3865 0.4296 0.0179  -0.0017 0.0823  88  LEU A CG  
655  C  CD1 . LEU A 88  ? 0.5173 0.3704 0.4108 0.0186  -0.0029 0.0788  88  LEU A CD1 
656  C  CD2 . LEU A 88  ? 0.4931 0.3586 0.4024 0.0129  -0.0062 0.0796  88  LEU A CD2 
657  N  N   . THR A 89  ? 0.4967 0.3788 0.4326 0.0169  0.0022  0.0961  89  THR A N   
658  C  CA  . THR A 89  ? 0.5001 0.3879 0.4451 0.0162  0.0034  0.0998  89  THR A CA  
659  C  C   . THR A 89  ? 0.4917 0.3813 0.4398 0.0119  -0.0008 0.0969  89  THR A C   
660  O  O   . THR A 89  ? 0.4827 0.3704 0.4272 0.0097  -0.0045 0.0923  89  THR A O   
661  C  CB  . THR A 89  ? 0.5124 0.4084 0.4675 0.0157  0.0042  0.1036  89  THR A CB  
662  O  OG1 . THR A 89  ? 0.5358 0.4358 0.4952 0.0114  -0.0004 0.1009  89  THR A OG1 
663  C  CG2 . THR A 89  ? 0.5117 0.4061 0.4636 0.0201  0.0079  0.1060  89  THR A CG2 
664  N  N   . SER A 90  ? 0.4780 0.3716 0.4333 0.0104  -0.0004 0.0996  90  SER A N   
665  C  CA  . SER A 90  ? 0.4869 0.3816 0.4450 0.0066  -0.0042 0.0971  90  SER A CA  
666  C  C   . SER A 90  ? 0.4988 0.3980 0.4614 0.0026  -0.0088 0.0942  90  SER A C   
667  O  O   . SER A 90  ? 0.5018 0.4004 0.4637 0.0000  -0.0125 0.0904  90  SER A O   
668  C  CB  . SER A 90  ? 0.5294 0.4274 0.4947 0.0055  -0.0026 0.1010  90  SER A CB  
669  O  OG  . SER A 90  ? 0.5921 0.4851 0.5522 0.0092  0.0016  0.1035  90  SER A OG  
670  N  N   . GLU A 91  ? 0.4514 0.3552 0.4184 0.0025  -0.0084 0.0959  91  GLU A N   
671  C  CA  . GLU A 91  ? 0.4703 0.3784 0.4414 -0.0010 -0.0123 0.0937  91  GLU A CA  
672  C  C   . GLU A 91  ? 0.4500 0.3534 0.4130 -0.0016 -0.0147 0.0885  91  GLU A C   
673  O  O   . GLU A 91  ? 0.4491 0.3551 0.4142 -0.0051 -0.0183 0.0858  91  GLU A O   
674  C  CB  . GLU A 91  ? 0.4623 0.3765 0.4403 -0.0006 -0.0111 0.0974  91  GLU A CB  
675  C  CG  . GLU A 91  ? 0.4747 0.3951 0.4625 -0.0018 -0.0099 0.1017  91  GLU A CG  
676  C  CD  . GLU A 91  ? 0.5511 0.4696 0.5386 0.0004  -0.0059 0.1048  91  GLU A CD  
677  O  OE1 . GLU A 91  ? 0.5436 0.4601 0.5280 0.0048  -0.0016 0.1074  91  GLU A OE1 
678  O  OE2 . GLU A 91  ? 0.5451 0.4633 0.5348 -0.0017 -0.0067 0.1048  91  GLU A OE2 
679  N  N   . ASP A 92  ? 0.4374 0.3341 0.3912 0.0013  -0.0129 0.0871  92  ASP A N   
680  C  CA  . ASP A 92  ? 0.3948 0.2871 0.3407 0.0006  -0.0150 0.0821  92  ASP A CA  
681  C  C   . ASP A 92  ? 0.4295 0.3197 0.3726 -0.0008 -0.0177 0.0780  92  ASP A C   
682  O  O   . ASP A 92  ? 0.4211 0.3093 0.3593 -0.0023 -0.0201 0.0734  92  ASP A O   
683  C  CB  . ASP A 92  ? 0.4256 0.3117 0.3628 0.0044  -0.0118 0.0825  92  ASP A CB  
684  C  CG  . ASP A 92  ? 0.4561 0.3435 0.3949 0.0065  -0.0091 0.0862  92  ASP A CG  
685  O  OD1 . ASP A 92  ? 0.4661 0.3577 0.4094 0.0040  -0.0112 0.0860  92  ASP A OD1 
686  O  OD2 . ASP A 92  ? 0.4830 0.3671 0.4184 0.0108  -0.0050 0.0893  92  ASP A OD2 
687  N  N   . SER A 93  ? 0.4023 0.2933 0.3487 -0.0007 -0.0175 0.0796  93  SER A N   
688  C  CA  . SER A 93  ? 0.4204 0.3095 0.3645 -0.0018 -0.0204 0.0758  93  SER A CA  
689  C  C   . SER A 93  ? 0.4346 0.3280 0.3828 -0.0061 -0.0246 0.0722  93  SER A C   
690  O  O   . SER A 93  ? 0.4204 0.3186 0.3762 -0.0085 -0.0256 0.0740  93  SER A O   
691  C  CB  . SER A 93  ? 0.4151 0.3037 0.3619 -0.0008 -0.0193 0.0787  93  SER A CB  
692  O  OG  . SER A 93  ? 0.4256 0.3093 0.3669 0.0031  -0.0154 0.0814  93  SER A OG  
693  N  N   . ALA A 94  ? 0.3993 0.2911 0.3428 -0.0070 -0.0272 0.0671  94  ALA A N   
694  C  CA  . ALA A 94  ? 0.3765 0.2721 0.3228 -0.0110 -0.0306 0.0634  94  ALA A CA  
695  C  C   . ALA A 94  ? 0.3717 0.2652 0.3117 -0.0114 -0.0325 0.0580  94  ALA A C   
696  O  O   . ALA A 94  ? 0.3980 0.2871 0.3315 -0.0086 -0.0313 0.0573  94  ALA A O   
697  C  CB  . ALA A 94  ? 0.3607 0.2588 0.3093 -0.0124 -0.0298 0.0651  94  ALA A CB  
698  N  N   . VAL A 95  ? 0.3725 0.2693 0.3145 -0.0148 -0.0356 0.0540  95  VAL A N   
699  C  CA  . VAL A 95  ? 0.3764 0.2724 0.3133 -0.0158 -0.0371 0.0488  95  VAL A CA  
700  C  C   . VAL A 95  ? 0.3771 0.2733 0.3122 -0.0179 -0.0365 0.0482  95  VAL A C   
701  O  O   . VAL A 95  ? 0.3573 0.2564 0.2970 -0.0200 -0.0367 0.0500  95  VAL A O   
702  C  CB  . VAL A 95  ? 0.3864 0.2860 0.3263 -0.0180 -0.0406 0.0446  95  VAL A CB  
703  C  CG1 . VAL A 95  ? 0.3784 0.2781 0.3136 -0.0190 -0.0421 0.0391  95  VAL A CG1 
704  C  CG2 . VAL A 95  ? 0.3694 0.2677 0.3103 -0.0156 -0.0413 0.0454  95  VAL A CG2 
705  N  N   . TYR A 96  ? 0.3550 0.2477 0.2830 -0.0175 -0.0357 0.0459  96  TYR A N   
706  C  CA  . TYR A 96  ? 0.3569 0.2484 0.2819 -0.0195 -0.0349 0.0454  96  TYR A CA  
707  C  C   . TYR A 96  ? 0.3629 0.2552 0.2846 -0.0225 -0.0369 0.0395  96  TYR A C   
708  O  O   . TYR A 96  ? 0.3867 0.2772 0.3040 -0.0214 -0.0374 0.0368  96  TYR A O   
709  C  CB  . TYR A 96  ? 0.3728 0.2584 0.2915 -0.0162 -0.0317 0.0481  96  TYR A CB  
710  C  CG  . TYR A 96  ? 0.3613 0.2467 0.2836 -0.0132 -0.0292 0.0540  96  TYR A CG  
711  C  CD1 . TYR A 96  ? 0.4104 0.2951 0.3339 -0.0100 -0.0281 0.0564  96  TYR A CD1 
712  C  CD2 . TYR A 96  ? 0.3482 0.2345 0.2728 -0.0135 -0.0280 0.0572  96  TYR A CD2 
713  C  CE1 . TYR A 96  ? 0.4115 0.2968 0.3390 -0.0077 -0.0256 0.0618  96  TYR A CE1 
714  C  CE2 . TYR A 96  ? 0.3665 0.2539 0.2954 -0.0108 -0.0257 0.0625  96  TYR A CE2 
715  C  CZ  . TYR A 96  ? 0.4003 0.2875 0.3309 -0.0081 -0.0245 0.0648  96  TYR A CZ  
716  O  OH  . TYR A 96  ? 0.4073 0.2962 0.3426 -0.0059 -0.0220 0.0699  96  TYR A OH  
717  N  N   . TYR A 97  ? 0.3702 0.2653 0.2937 -0.0264 -0.0380 0.0377  97  TYR A N   
718  C  CA  . TYR A 97  ? 0.3637 0.2603 0.2847 -0.0298 -0.0397 0.0321  97  TYR A CA  
719  C  C   . TYR A 97  ? 0.3605 0.2532 0.2754 -0.0317 -0.0381 0.0318  97  TYR A C   
720  O  O   . TYR A 97  ? 0.3884 0.2792 0.3034 -0.0315 -0.0367 0.0354  97  TYR A O   
721  C  CB  . TYR A 97  ? 0.3787 0.2809 0.3057 -0.0331 -0.0419 0.0303  97  TYR A CB  
722  C  CG  . TYR A 97  ? 0.3383 0.2442 0.2710 -0.0318 -0.0438 0.0301  97  TYR A CG  
723  C  CD1 . TYR A 97  ? 0.3512 0.2595 0.2839 -0.0317 -0.0457 0.0256  97  TYR A CD1 
724  C  CD2 . TYR A 97  ? 0.3640 0.2706 0.3017 -0.0304 -0.0436 0.0344  97  TYR A CD2 
725  C  CE1 . TYR A 97  ? 0.3656 0.2760 0.3025 -0.0299 -0.0473 0.0256  97  TYR A CE1 
726  C  CE2 . TYR A 97  ? 0.3625 0.2712 0.3046 -0.0292 -0.0451 0.0343  97  TYR A CE2 
727  C  CZ  . TYR A 97  ? 0.3675 0.2775 0.3087 -0.0287 -0.0469 0.0300  97  TYR A CZ  
728  O  OH  . TYR A 97  ? 0.3768 0.2881 0.3219 -0.0274 -0.0485 0.0302  97  TYR A OH  
729  N  N   . CYS A 98  ? 0.3843 0.2759 0.2942 -0.0337 -0.0385 0.0274  98  CYS A N   
730  C  CA  . CYS A 98  ? 0.3872 0.2760 0.2921 -0.0371 -0.0376 0.0259  98  CYS A CA  
731  C  C   . CYS A 98  ? 0.3943 0.2883 0.3019 -0.0419 -0.0395 0.0215  98  CYS A C   
732  O  O   . CYS A 98  ? 0.3564 0.2557 0.2680 -0.0425 -0.0415 0.0182  98  CYS A O   
733  C  CB  . CYS A 98  ? 0.3871 0.2700 0.2834 -0.0369 -0.0363 0.0243  98  CYS A CB  
734  S  SG  . CYS A 98  ? 0.4829 0.3697 0.3790 -0.0379 -0.0387 0.0184  98  CYS A SG  
735  N  N   . ALA A 99  ? 0.3671 0.2598 0.2728 -0.0452 -0.0388 0.0216  99  ALA A N   
736  C  CA  . ALA A 99  ? 0.3633 0.2611 0.2719 -0.0497 -0.0403 0.0178  99  ALA A CA  
737  C  C   . ALA A 99  ? 0.3943 0.2884 0.2973 -0.0537 -0.0390 0.0170  99  ALA A C   
738  O  O   . ALA A 99  ? 0.4094 0.2977 0.3083 -0.0526 -0.0374 0.0208  99  ALA A O   
739  C  CB  . ALA A 99  ? 0.3541 0.2564 0.2702 -0.0491 -0.0417 0.0197  99  ALA A CB  
740  N  N   . ARG A 100 ? 0.3700 0.2674 0.2728 -0.0583 -0.0397 0.0123  100 ARG A N   
741  C  CA  . ARG A 100 ? 0.3787 0.2739 0.2781 -0.0625 -0.0388 0.0120  100 ARG A CA  
742  C  C   . ARG A 100 ? 0.3795 0.2793 0.2852 -0.0628 -0.0403 0.0132  100 ARG A C   
743  O  O   . ARG A 100 ? 0.3692 0.2756 0.2806 -0.0636 -0.0420 0.0103  100 ARG A O   
744  C  CB  . ARG A 100 ? 0.3776 0.2743 0.2737 -0.0676 -0.0385 0.0064  100 ARG A CB  
745  C  CG  . ARG A 100 ? 0.4054 0.2969 0.2948 -0.0673 -0.0372 0.0055  100 ARG A CG  
746  C  CD  . ARG A 100 ? 0.4038 0.2958 0.2890 -0.0731 -0.0365 0.0004  100 ARG A CD  
747  N  NE  . ARG A 100 ? 0.4293 0.3306 0.3209 -0.0759 -0.0380 -0.0040 100 ARG A NE  
748  C  CZ  . ARG A 100 ? 0.5082 0.4143 0.4001 -0.0794 -0.0382 -0.0093 100 ARG A CZ  
749  N  NH1 . ARG A 100 ? 0.5994 0.5014 0.4852 -0.0812 -0.0373 -0.0110 100 ARG A NH1 
750  N  NH2 . ARG A 100 ? 0.4707 0.3854 0.3686 -0.0816 -0.0393 -0.0131 100 ARG A NH2 
751  N  N   . LEU A 101 ? 0.3638 0.2598 0.2682 -0.0621 -0.0398 0.0174  101 LEU A N   
752  C  CA  . LEU A 101 ? 0.4026 0.3025 0.3131 -0.0619 -0.0415 0.0193  101 LEU A CA  
753  C  C   . LEU A 101 ? 0.4111 0.3115 0.3198 -0.0665 -0.0418 0.0173  101 LEU A C   
754  O  O   . LEU A 101 ? 0.4083 0.3131 0.3220 -0.0674 -0.0435 0.0168  101 LEU A O   
755  C  CB  . LEU A 101 ? 0.4050 0.3031 0.3180 -0.0578 -0.0415 0.0252  101 LEU A CB  
756  C  CG  . LEU A 101 ? 0.4020 0.3012 0.3189 -0.0532 -0.0415 0.0274  101 LEU A CG  
757  C  CD1 . LEU A 101 ? 0.3760 0.2736 0.2952 -0.0499 -0.0411 0.0334  101 LEU A CD1 
758  C  CD2 . LEU A 101 ? 0.4191 0.3248 0.3427 -0.0532 -0.0435 0.0248  101 LEU A CD2 
759  N  N   . ASP A 102 ? 0.4296 0.3254 0.3309 -0.0697 -0.0402 0.0158  102 ASP A N   
760  C  CA  . ASP A 102 ? 0.4401 0.3362 0.3395 -0.0741 -0.0404 0.0140  102 ASP A CA  
761  C  C   . ASP A 102 ? 0.4307 0.3344 0.3350 -0.0766 -0.0414 0.0089  102 ASP A C   
762  O  O   . ASP A 102 ? 0.4332 0.3397 0.3383 -0.0769 -0.0411 0.0055  102 ASP A O   
763  C  CB  . ASP A 102 ? 0.4914 0.3808 0.3814 -0.0775 -0.0382 0.0129  102 ASP A CB  
764  C  CG  . ASP A 102 ? 0.5613 0.4425 0.4455 -0.0749 -0.0372 0.0179  102 ASP A CG  
765  O  OD1 . ASP A 102 ? 0.5979 0.4794 0.4855 -0.0720 -0.0384 0.0221  102 ASP A OD1 
766  O  OD2 . ASP A 102 ? 0.7048 0.5796 0.5814 -0.0760 -0.0352 0.0174  102 ASP A OD2 
767  N  N   . TRP A 103 ? 0.4063 0.3132 0.3136 -0.0783 -0.0428 0.0083  103 TRP A N   
768  C  CA  . TRP A 103 ? 0.3964 0.3106 0.3093 -0.0794 -0.0439 0.0040  103 TRP A CA  
769  C  C   . TRP A 103 ? 0.4025 0.3190 0.3129 -0.0831 -0.0424 -0.0013 103 TRP A C   
770  O  O   . TRP A 103 ? 0.4050 0.3275 0.3198 -0.0826 -0.0431 -0.0049 103 TRP A O   
771  C  CB  . TRP A 103 ? 0.3795 0.2959 0.2950 -0.0809 -0.0455 0.0040  103 TRP A CB  
772  C  CG  . TRP A 103 ? 0.4215 0.3346 0.3308 -0.0853 -0.0444 0.0032  103 TRP A CG  
773  C  CD1 . TRP A 103 ? 0.4530 0.3608 0.3584 -0.0855 -0.0447 0.0070  103 TRP A CD1 
774  C  CD2 . TRP A 103 ? 0.4041 0.3193 0.3106 -0.0901 -0.0430 -0.0017 103 TRP A CD2 
775  N  NE1 . TRP A 103 ? 0.4940 0.3996 0.3936 -0.0900 -0.0435 0.0048  103 TRP A NE1 
776  C  CE2 . TRP A 103 ? 0.4636 0.3736 0.3637 -0.0931 -0.0423 -0.0005 103 TRP A CE2 
777  C  CE3 . TRP A 103 ? 0.4043 0.3255 0.3133 -0.0920 -0.0422 -0.0071 103 TRP A CE3 
778  C  CZ2 . TRP A 103 ? 0.5043 0.4145 0.4000 -0.0982 -0.0405 -0.0044 103 TRP A CZ2 
779  C  CZ3 . TRP A 103 ? 0.4137 0.3359 0.3190 -0.0970 -0.0405 -0.0110 103 TRP A CZ3 
780  C  CH2 . TRP A 103 ? 0.4680 0.3845 0.3666 -0.1002 -0.0395 -0.0096 103 TRP A CH2 
781  N  N   . TYR A 104 ? 0.3835 0.2954 0.2866 -0.0870 -0.0405 -0.0020 104 TYR A N   
782  C  CA  . TYR A 104 ? 0.3796 0.2941 0.2805 -0.0914 -0.0389 -0.0073 104 TYR A CA  
783  C  C   . TYR A 104 ? 0.3914 0.3063 0.2919 -0.0902 -0.0383 -0.0088 104 TYR A C   
784  O  O   . TYR A 104 ? 0.4258 0.3451 0.3266 -0.0933 -0.0376 -0.0136 104 TYR A O   
785  C  CB  . TYR A 104 ? 0.4260 0.3351 0.3188 -0.0964 -0.0368 -0.0077 104 TYR A CB  
786  C  CG  . TYR A 104 ? 0.3916 0.2913 0.2781 -0.0949 -0.0363 -0.0024 104 TYR A CG  
787  C  CD1 . TYR A 104 ? 0.4234 0.3171 0.3046 -0.0940 -0.0350 -0.0010 104 TYR A CD1 
788  C  CD2 . TYR A 104 ? 0.4071 0.3040 0.2927 -0.0942 -0.0373 0.0009  104 TYR A CD2 
789  C  CE1 . TYR A 104 ? 0.4453 0.3304 0.3206 -0.0920 -0.0345 0.0038  104 TYR A CE1 
790  C  CE2 . TYR A 104 ? 0.4534 0.3422 0.3334 -0.0923 -0.0370 0.0058  104 TYR A CE2 
791  C  CZ  . TYR A 104 ? 0.4505 0.3334 0.3254 -0.0911 -0.0355 0.0071  104 TYR A CZ  
792  O  OH  . TYR A 104 ? 0.5686 0.4431 0.4374 -0.0891 -0.0349 0.0116  104 TYR A OH  
793  N  N   . PHE A 105 ? 0.3831 0.2935 0.2826 -0.0860 -0.0386 -0.0049 105 PHE A N   
794  C  CA  . PHE A 105 ? 0.3766 0.2872 0.2755 -0.0845 -0.0384 -0.0062 105 PHE A CA  
795  C  C   . PHE A 105 ? 0.3842 0.2988 0.2899 -0.0790 -0.0405 -0.0049 105 PHE A C   
796  O  O   . PHE A 105 ? 0.3738 0.2869 0.2783 -0.0766 -0.0405 -0.0046 105 PHE A O   
797  C  CB  . PHE A 105 ? 0.4151 0.3166 0.3058 -0.0842 -0.0367 -0.0036 105 PHE A CB  
798  C  CG  . PHE A 105 ? 0.4195 0.3152 0.3021 -0.0895 -0.0345 -0.0044 105 PHE A CG  
799  C  CD1 . PHE A 105 ? 0.4297 0.3296 0.3120 -0.0951 -0.0337 -0.0094 105 PHE A CD1 
800  C  CD2 . PHE A 105 ? 0.4408 0.3269 0.3161 -0.0887 -0.0333 -0.0002 105 PHE A CD2 
801  C  CE1 . PHE A 105 ? 0.4249 0.3190 0.2992 -0.1002 -0.0315 -0.0102 105 PHE A CE1 
802  C  CE2 . PHE A 105 ? 0.4280 0.3077 0.2948 -0.0936 -0.0312 -0.0010 105 PHE A CE2 
803  C  CZ  . PHE A 105 ? 0.4368 0.3205 0.3032 -0.0994 -0.0304 -0.0058 105 PHE A CZ  
804  N  N   . ASP A 106 ? 0.3769 0.2959 0.2889 -0.0772 -0.0422 -0.0042 106 ASP A N   
805  C  CA  . ASP A 106 ? 0.3652 0.2858 0.2826 -0.0720 -0.0439 -0.0016 106 ASP A CA  
806  C  C   . ASP A 106 ? 0.3870 0.3105 0.3057 -0.0699 -0.0444 -0.0042 106 ASP A C   
807  O  O   . ASP A 106 ? 0.3788 0.3081 0.2995 -0.0719 -0.0450 -0.0092 106 ASP A O   
808  C  CB  . ASP A 106 ? 0.3399 0.2662 0.2638 -0.0716 -0.0457 -0.0027 106 ASP A CB  
809  C  CG  . ASP A 106 ? 0.3438 0.2715 0.2732 -0.0666 -0.0475 -0.0001 106 ASP A CG  
810  O  OD1 . ASP A 106 ? 0.3981 0.3217 0.3273 -0.0643 -0.0473 0.0048  106 ASP A OD1 
811  O  OD2 . ASP A 106 ? 0.3720 0.3049 0.3057 -0.0651 -0.0489 -0.0031 106 ASP A OD2 
812  N  N   . LEU A 107 ? 0.3458 0.2655 0.2636 -0.0657 -0.0444 -0.0008 107 LEU A N   
813  C  CA  . LEU A 107 ? 0.3479 0.2690 0.2659 -0.0631 -0.0451 -0.0025 107 LEU A CA  
814  C  C   . LEU A 107 ? 0.3798 0.2967 0.2981 -0.0579 -0.0451 0.0025  107 LEU A C   
815  O  O   . LEU A 107 ? 0.3691 0.2799 0.2836 -0.0570 -0.0435 0.0066  107 LEU A O   
816  C  CB  . LEU A 107 ? 0.3609 0.2790 0.2723 -0.0659 -0.0437 -0.0050 107 LEU A CB  
817  C  CG  . LEU A 107 ? 0.3820 0.3012 0.2926 -0.0637 -0.0446 -0.0072 107 LEU A CG  
818  C  CD1 . LEU A 107 ? 0.4155 0.3438 0.3322 -0.0640 -0.0467 -0.0120 107 LEU A CD1 
819  C  CD2 . LEU A 107 ? 0.4231 0.3376 0.3261 -0.0671 -0.0430 -0.0088 107 LEU A CD2 
820  N  N   . TRP A 108 ? 0.3697 0.2898 0.2922 -0.0542 -0.0468 0.0021  108 TRP A N   
821  C  CA  . TRP A 108 ? 0.3760 0.2923 0.2988 -0.0494 -0.0466 0.0069  108 TRP A CA  
822  C  C   . TRP A 108 ? 0.3724 0.2883 0.2935 -0.0463 -0.0472 0.0055  108 TRP A C   
823  O  O   . TRP A 108 ? 0.3786 0.2996 0.3017 -0.0467 -0.0490 0.0010  108 TRP A O   
824  C  CB  . TRP A 108 ? 0.3626 0.2821 0.2921 -0.0476 -0.0480 0.0087  108 TRP A CB  
825  C  CG  . TRP A 108 ? 0.3831 0.3027 0.3146 -0.0500 -0.0478 0.0107  108 TRP A CG  
826  C  CD1 . TRP A 108 ? 0.3350 0.2572 0.2669 -0.0542 -0.0481 0.0080  108 TRP A CD1 
827  C  CD2 . TRP A 108 ? 0.3709 0.2876 0.3041 -0.0481 -0.0472 0.0162  108 TRP A CD2 
828  N  NE1 . TRP A 108 ? 0.3352 0.2560 0.2685 -0.0549 -0.0480 0.0114  108 TRP A NE1 
829  C  CE2 . TRP A 108 ? 0.3603 0.2782 0.2949 -0.0513 -0.0476 0.0164  108 TRP A CE2 
830  C  CE3 . TRP A 108 ? 0.3695 0.2833 0.3035 -0.0441 -0.0465 0.0210  108 TRP A CE3 
831  C  CZ2 . TRP A 108 ? 0.3619 0.2785 0.2988 -0.0506 -0.0476 0.0211  108 TRP A CZ2 
832  C  CZ3 . TRP A 108 ? 0.3750 0.2879 0.3118 -0.0436 -0.0461 0.0255  108 TRP A CZ3 
833  C  CH2 . TRP A 108 ? 0.3727 0.2872 0.3112 -0.0467 -0.0469 0.0255  108 TRP A CH2 
834  N  N   . GLY A 109 ? 0.3657 0.2757 0.2830 -0.0430 -0.0458 0.0094  109 GLY A N   
835  C  CA  . GLY A 109 ? 0.3557 0.2646 0.2717 -0.0391 -0.0465 0.0093  109 GLY A CA  
836  C  C   . GLY A 109 ? 0.3680 0.2796 0.2898 -0.0357 -0.0480 0.0109  109 GLY A C   
837  O  O   . GLY A 109 ? 0.3783 0.2918 0.3048 -0.0365 -0.0483 0.0127  109 GLY A O   
838  N  N   . ALA A 110 ? 0.3594 0.2705 0.2801 -0.0321 -0.0492 0.0101  110 ALA A N   
839  C  CA  . ALA A 110 ? 0.3798 0.2925 0.3052 -0.0290 -0.0505 0.0117  110 ALA A CA  
840  C  C   . ALA A 110 ? 0.3658 0.2736 0.2912 -0.0261 -0.0486 0.0178  110 ALA A C   
841  O  O   . ALA A 110 ? 0.3788 0.2871 0.3082 -0.0240 -0.0493 0.0200  110 ALA A O   
842  C  CB  . ALA A 110 ? 0.3851 0.2992 0.3091 -0.0264 -0.0527 0.0084  110 ALA A CB  
843  N  N   . GLY A 111 ? 0.3596 0.2625 0.2806 -0.0257 -0.0461 0.0208  111 GLY A N   
844  C  CA  . GLY A 111 ? 0.3523 0.2515 0.2739 -0.0231 -0.0439 0.0267  111 GLY A CA  
845  C  C   . GLY A 111 ? 0.3736 0.2681 0.2909 -0.0186 -0.0429 0.0287  111 GLY A C   
846  O  O   . GLY A 111 ? 0.4213 0.3165 0.3375 -0.0170 -0.0449 0.0259  111 GLY A O   
847  N  N   . THR A 112 ? 0.3840 0.2736 0.2985 -0.0164 -0.0399 0.0333  112 THR A N   
848  C  CA  . THR A 112 ? 0.3814 0.2659 0.2914 -0.0121 -0.0383 0.0360  112 THR A CA  
849  C  C   . THR A 112 ? 0.3854 0.2701 0.3004 -0.0101 -0.0368 0.0412  112 THR A C   
850  O  O   . THR A 112 ? 0.4023 0.2876 0.3203 -0.0110 -0.0350 0.0445  112 THR A O   
851  C  CB  . THR A 112 ? 0.4238 0.3024 0.3261 -0.0109 -0.0357 0.0370  112 THR A CB  
852  O  OG1 . THR A 112 ? 0.4191 0.2978 0.3170 -0.0133 -0.0374 0.0318  112 THR A OG1 
853  C  CG2 . THR A 112 ? 0.4239 0.2970 0.3215 -0.0062 -0.0337 0.0401  112 THR A CG2 
854  N  N   . THR A 113 ? 0.3776 0.2616 0.2933 -0.0076 -0.0376 0.0418  113 THR A N   
855  C  CA  . THR A 113 ? 0.3815 0.2648 0.3011 -0.0057 -0.0357 0.0470  113 THR A CA  
856  C  C   . THR A 113 ? 0.4110 0.2888 0.3255 -0.0023 -0.0320 0.0510  113 THR A C   
857  O  O   . THR A 113 ? 0.4504 0.3238 0.3582 0.0003  -0.0317 0.0500  113 THR A O   
858  C  CB  . THR A 113 ? 0.4102 0.2936 0.3311 -0.0042 -0.0378 0.0461  113 THR A CB  
859  O  OG1 . THR A 113 ? 0.3889 0.2773 0.3149 -0.0072 -0.0409 0.0427  113 THR A OG1 
860  C  CG2 . THR A 113 ? 0.4029 0.2848 0.3271 -0.0026 -0.0357 0.0514  113 THR A CG2 
861  N  N   . VAL A 114 ? 0.4026 0.2808 0.3203 -0.0022 -0.0291 0.0554  114 VAL A N   
862  C  CA  . VAL A 114 ? 0.4112 0.2847 0.3246 0.0012  -0.0252 0.0595  114 VAL A CA  
863  C  C   . VAL A 114 ? 0.4222 0.2967 0.3408 0.0026  -0.0235 0.0641  114 VAL A C   
864  O  O   . VAL A 114 ? 0.4171 0.2964 0.3436 0.0004  -0.0238 0.0661  114 VAL A O   
865  C  CB  . VAL A 114 ? 0.4268 0.3004 0.3404 0.0007  -0.0229 0.0616  114 VAL A CB  
866  C  CG1 . VAL A 114 ? 0.4559 0.3252 0.3662 0.0047  -0.0185 0.0663  114 VAL A CG1 
867  C  CG2 . VAL A 114 ? 0.4178 0.2897 0.3257 -0.0011 -0.0244 0.0571  114 VAL A CG2 
868  N  N   . THR A 115 ? 0.4036 0.2731 0.3173 0.0061  -0.0218 0.0657  115 THR A N   
869  C  CA  . THR A 115 ? 0.4103 0.2801 0.3281 0.0073  -0.0202 0.0699  115 THR A CA  
870  C  C   . THR A 115 ? 0.4457 0.3118 0.3604 0.0107  -0.0152 0.0746  115 THR A C   
871  O  O   . THR A 115 ? 0.4356 0.2957 0.3418 0.0139  -0.0138 0.0742  115 THR A O   
872  C  CB  . THR A 115 ? 0.4247 0.2914 0.3391 0.0085  -0.0223 0.0679  115 THR A CB  
873  O  OG1 . THR A 115 ? 0.4232 0.2937 0.3407 0.0056  -0.0267 0.0633  115 THR A OG1 
874  C  CG2 . THR A 115 ? 0.4164 0.2827 0.3347 0.0091  -0.0207 0.0720  115 THR A CG2 
875  N  N   . VAL A 116 ? 0.4369 0.3069 0.3582 0.0102  -0.0126 0.0788  116 VAL A N   
876  C  CA  . VAL A 116 ? 0.4410 0.3085 0.3602 0.0136  -0.0076 0.0834  116 VAL A CA  
877  C  C   . VAL A 116 ? 0.4733 0.3398 0.3945 0.0147  -0.0057 0.0868  116 VAL A C   
878  O  O   . VAL A 116 ? 0.4682 0.3396 0.3978 0.0121  -0.0064 0.0886  116 VAL A O   
879  C  CB  . VAL A 116 ? 0.4784 0.3511 0.4043 0.0128  -0.0058 0.0863  116 VAL A CB  
880  C  CG1 . VAL A 116 ? 0.5144 0.3848 0.4382 0.0169  -0.0003 0.0911  116 VAL A CG1 
881  C  CG2 . VAL A 116 ? 0.4591 0.3320 0.3825 0.0113  -0.0080 0.0828  116 VAL A CG2 
882  N  N   . SER A 117 ? 0.4642 0.3237 0.3768 0.0184  -0.0034 0.0875  117 SER A N   
883  C  CA  . SER A 117 ? 0.4687 0.3251 0.3801 0.0194  -0.0026 0.0893  117 SER A CA  
884  C  C   . SER A 117 ? 0.5274 0.3802 0.4355 0.0231  0.0031  0.0942  117 SER A C   
885  O  O   . SER A 117 ? 0.5270 0.3745 0.4267 0.0265  0.0053  0.0940  117 SER A O   
886  C  CB  . SER A 117 ? 0.4467 0.2978 0.3500 0.0204  -0.0062 0.0848  117 SER A CB  
887  O  OG  . SER A 117 ? 0.4732 0.3194 0.3728 0.0222  -0.0055 0.0863  117 SER A OG  
888  N  N   . ALA A 118 ? 0.5201 0.3759 0.4351 0.0222  0.0057  0.0986  118 ALA A N   
889  C  CA  . ALA A 118 ? 0.5409 0.3935 0.4532 0.0253  0.0114  0.1034  118 ALA A CA  
890  C  C   . ALA A 118 ? 0.6073 0.4618 0.5258 0.0232  0.0125  0.1067  118 ALA A C   
891  O  O   . ALA A 118 ? 0.5730 0.4350 0.5021 0.0199  0.0123  0.1085  118 ALA A O   
892  C  CB  . ALA A 118 ? 0.5655 0.4222 0.4815 0.0268  0.0154  0.1064  118 ALA A CB  
893  N  N   . ALA A 119 ? 0.6563 0.5035 0.5676 0.0250  0.0135  0.1074  119 ALA A N   
894  C  CA  . ALA A 119 ? 0.7251 0.5724 0.6406 0.0225  0.0137  0.1097  119 ALA A CA  
895  C  C   . ALA A 119 ? 0.7942 0.6456 0.7167 0.0220  0.0194  0.1157  119 ALA A C   
896  O  O   . ALA A 119 ? 0.7828 0.6363 0.7114 0.0188  0.0196  0.1179  119 ALA A O   
897  C  CB  . ALA A 119 ? 0.7553 0.5930 0.6603 0.0248  0.0128  0.1085  119 ALA A CB  
898  N  N   . GLY A 120 ? 0.8012 0.6535 0.7225 0.0251  0.0241  0.1181  120 GLY A N   
899  C  CA  . GLY A 120 ? 1.0697 0.9263 0.9972 0.0253  0.0301  0.1238  120 GLY A CA  
900  C  C   . GLY A 120 ? 1.1310 0.9797 1.0505 0.0280  0.0349  0.1269  120 GLY A C   
901  O  O   . GLY A 120 ? 1.0410 0.8887 0.9629 0.0253  0.0353  0.1289  120 GLY A O   
902  N  N   . SER A 134 ? 0.6585 0.6040 0.6501 -0.0257 -0.0567 0.0946  134 SER A N   
903  C  CA  . SER A 134 ? 0.6392 0.5784 0.6217 -0.0288 -0.0590 0.0911  134 SER A CA  
904  C  C   . SER A 134 ? 0.5675 0.5002 0.5427 -0.0318 -0.0573 0.0862  134 SER A C   
905  O  O   . SER A 134 ? 0.5757 0.5033 0.5433 -0.0348 -0.0587 0.0829  134 SER A O   
906  C  CB  . SER A 134 ? 0.7100 0.6443 0.6852 -0.0254 -0.0588 0.0928  134 SER A CB  
907  O  OG  . SER A 134 ? 0.7392 0.6673 0.7081 -0.0216 -0.0544 0.0932  134 SER A OG  
908  N  N   . ASP A 135 ? 0.5657 0.4986 0.5428 -0.0310 -0.0544 0.0854  135 ASP A N   
909  C  CA  . ASP A 135 ? 0.5508 0.4790 0.5223 -0.0342 -0.0537 0.0805  135 ASP A CA  
910  C  C   . ASP A 135 ? 0.4996 0.4310 0.4746 -0.0392 -0.0573 0.0778  135 ASP A C   
911  O  O   . ASP A 135 ? 0.4964 0.4344 0.4800 -0.0400 -0.0594 0.0799  135 ASP A O   
912  C  CB  . ASP A 135 ? 0.5531 0.4810 0.5261 -0.0325 -0.0504 0.0802  135 ASP A CB  
913  C  CG  . ASP A 135 ? 0.6717 0.5951 0.6398 -0.0276 -0.0465 0.0821  135 ASP A CG  
914  O  OD1 . ASP A 135 ? 0.6770 0.5967 0.6397 -0.0257 -0.0462 0.0834  135 ASP A OD1 
915  O  OD2 . ASP A 135 ? 0.6561 0.5794 0.6256 -0.0256 -0.0437 0.0825  135 ASP A OD2 
916  N  N   . ILE A 136 ? 0.4259 0.3530 0.3944 -0.0427 -0.0578 0.0730  136 ILE A N   
917  C  CA  . ILE A 136 ? 0.4057 0.3357 0.3773 -0.0471 -0.0610 0.0704  136 ILE A CA  
918  C  C   . ILE A 136 ? 0.4515 0.3846 0.4290 -0.0475 -0.0603 0.0696  136 ILE A C   
919  O  O   . ILE A 136 ? 0.4503 0.3807 0.4251 -0.0463 -0.0576 0.0679  136 ILE A O   
920  C  CB  . ILE A 136 ? 0.4120 0.3367 0.3749 -0.0505 -0.0615 0.0657  136 ILE A CB  
921  C  CG1 . ILE A 136 ? 0.4558 0.3767 0.4122 -0.0501 -0.0622 0.0670  136 ILE A CG1 
922  C  CG2 . ILE A 136 ? 0.4517 0.3789 0.4171 -0.0549 -0.0644 0.0625  136 ILE A CG2 
923  C  CD1 . ILE A 136 ? 0.4917 0.4074 0.4393 -0.0538 -0.0626 0.0626  136 ILE A CD1 
924  N  N   . VAL A 137 ? 0.4145 0.3530 0.4001 -0.0492 -0.0629 0.0709  137 VAL A N   
925  C  CA  . VAL A 137 ? 0.4127 0.3534 0.4033 -0.0499 -0.0625 0.0701  137 VAL A CA  
926  C  C   . VAL A 137 ? 0.4226 0.3621 0.4112 -0.0541 -0.0648 0.0654  137 VAL A C   
927  O  O   . VAL A 137 ? 0.4198 0.3601 0.4083 -0.0569 -0.0679 0.0646  137 VAL A O   
928  C  CB  . VAL A 137 ? 0.4226 0.3697 0.4232 -0.0494 -0.0636 0.0745  137 VAL A CB  
929  C  CG1 . VAL A 137 ? 0.4177 0.3663 0.4231 -0.0505 -0.0633 0.0738  137 VAL A CG1 
930  C  CG2 . VAL A 137 ? 0.4792 0.4283 0.4821 -0.0450 -0.0612 0.0792  137 VAL A CG2 
931  N  N   . LEU A 138 ? 0.3853 0.3227 0.3722 -0.0542 -0.0634 0.0622  138 LEU A N   
932  C  CA  . LEU A 138 ? 0.3844 0.3210 0.3701 -0.0574 -0.0652 0.0577  138 LEU A CA  
933  C  C   . LEU A 138 ? 0.3811 0.3199 0.3731 -0.0576 -0.0658 0.0584  138 LEU A C   
934  O  O   . LEU A 138 ? 0.4050 0.3435 0.3984 -0.0550 -0.0633 0.0596  138 LEU A O   
935  C  CB  . LEU A 138 ? 0.3864 0.3191 0.3653 -0.0572 -0.0632 0.0533  138 LEU A CB  
936  C  CG  . LEU A 138 ? 0.4168 0.3463 0.3884 -0.0574 -0.0621 0.0522  138 LEU A CG  
937  C  CD1 . LEU A 138 ? 0.4294 0.3558 0.3950 -0.0579 -0.0603 0.0475  138 LEU A CD1 
938  C  CD2 . LEU A 138 ? 0.4263 0.3557 0.3959 -0.0603 -0.0648 0.0518  138 LEU A CD2 
939  N  N   . THR A 139 ? 0.3697 0.3101 0.3646 -0.0609 -0.0690 0.0574  139 THR A N   
940  C  CA  . THR A 139 ? 0.3653 0.3069 0.3655 -0.0617 -0.0699 0.0579  139 THR A CA  
941  C  C   . THR A 139 ? 0.3474 0.2862 0.3441 -0.0637 -0.0712 0.0526  139 THR A C   
942  O  O   . THR A 139 ? 0.4030 0.3411 0.3970 -0.0665 -0.0735 0.0501  139 THR A O   
943  C  CB  . THR A 139 ? 0.4059 0.3513 0.4125 -0.0639 -0.0727 0.0611  139 THR A CB  
944  O  OG1 . THR A 139 ? 0.4199 0.3683 0.4293 -0.0615 -0.0714 0.0656  139 THR A OG1 
945  C  CG2 . THR A 139 ? 0.4286 0.3747 0.4405 -0.0650 -0.0734 0.0620  139 THR A CG2 
946  N  N   . GLN A 140 ? 0.3274 0.2644 0.3240 -0.0622 -0.0697 0.0512  140 GLN A N   
947  C  CA  . GLN A 140 ? 0.3421 0.2768 0.3361 -0.0635 -0.0709 0.0464  140 GLN A CA  
948  C  C   . GLN A 140 ? 0.3730 0.3076 0.3714 -0.0651 -0.0730 0.0473  140 GLN A C   
949  O  O   . GLN A 140 ? 0.3829 0.3186 0.3860 -0.0642 -0.0722 0.0513  140 GLN A O   
950  C  CB  . GLN A 140 ? 0.3585 0.2912 0.3491 -0.0607 -0.0685 0.0438  140 GLN A CB  
951  C  CG  . GLN A 140 ? 0.3698 0.3023 0.3560 -0.0593 -0.0663 0.0431  140 GLN A CG  
952  C  CD  . GLN A 140 ? 0.3917 0.3225 0.3741 -0.0570 -0.0644 0.0398  140 GLN A CD  
953  O  OE1 . GLN A 140 ? 0.3772 0.3074 0.3566 -0.0553 -0.0622 0.0403  140 GLN A OE1 
954  N  NE2 . GLN A 140 ? 0.3887 0.3187 0.3707 -0.0569 -0.0653 0.0363  140 GLN A NE2 
955  N  N   . SER A 141 ? 0.3574 0.2902 0.3538 -0.0675 -0.0752 0.0435  141 SER A N   
956  C  CA  . SER A 141 ? 0.3682 0.2996 0.3676 -0.0693 -0.0774 0.0439  141 SER A CA  
957  C  C   . SER A 141 ? 0.3731 0.3012 0.3683 -0.0696 -0.0783 0.0385  141 SER A C   
958  O  O   . SER A 141 ? 0.4126 0.3406 0.4038 -0.0708 -0.0790 0.0350  141 SER A O   
959  C  CB  . SER A 141 ? 0.3866 0.3201 0.3888 -0.0729 -0.0803 0.0458  141 SER A CB  
960  O  OG  . SER A 141 ? 0.4543 0.3860 0.4591 -0.0751 -0.0825 0.0460  141 SER A OG  
961  N  N   . PRO A 142 ? 0.3615 0.2865 0.3569 -0.0683 -0.0782 0.0375  142 PRO A N   
962  C  CA  . PRO A 142 ? 0.3938 0.3181 0.3927 -0.0666 -0.0768 0.0414  142 PRO A CA  
963  C  C   . PRO A 142 ? 0.4137 0.3388 0.4115 -0.0626 -0.0735 0.0422  142 PRO A C   
964  O  O   . PRO A 142 ? 0.3832 0.3091 0.3773 -0.0614 -0.0725 0.0395  142 PRO A O   
965  C  CB  . PRO A 142 ? 0.4068 0.3263 0.4037 -0.0663 -0.0779 0.0385  142 PRO A CB  
966  C  CG  . PRO A 142 ? 0.4097 0.3286 0.4015 -0.0653 -0.0781 0.0328  142 PRO A CG  
967  C  CD  . PRO A 142 ? 0.4042 0.3261 0.3955 -0.0681 -0.0791 0.0324  142 PRO A CD  
968  N  N   . THR A 143 ? 0.4071 0.3317 0.4076 -0.0608 -0.0717 0.0460  143 THR A N   
969  C  CA  . THR A 143 ? 0.4028 0.3274 0.4014 -0.0569 -0.0687 0.0467  143 THR A CA  
970  C  C   . THR A 143 ? 0.3870 0.3076 0.3820 -0.0541 -0.0682 0.0437  143 THR A C   
971  O  O   . THR A 143 ? 0.3991 0.3193 0.3913 -0.0509 -0.0662 0.0430  143 THR A O   
972  C  CB  . THR A 143 ? 0.4644 0.3908 0.4670 -0.0557 -0.0664 0.0523  143 THR A CB  
973  O  OG1 . THR A 143 ? 0.5555 0.4799 0.5611 -0.0569 -0.0671 0.0544  143 THR A OG1 
974  C  CG2 . THR A 143 ? 0.4521 0.3828 0.4587 -0.0580 -0.0671 0.0555  143 THR A CG2 
975  N  N   . SER A 144 ? 0.4032 0.3206 0.3980 -0.0552 -0.0702 0.0421  144 SER A N   
976  C  CA  . SER A 144 ? 0.4160 0.3297 0.4068 -0.0525 -0.0703 0.0384  144 SER A CA  
977  C  C   . SER A 144 ? 0.4320 0.3430 0.4217 -0.0545 -0.0731 0.0351  144 SER A C   
978  O  O   . SER A 144 ? 0.4299 0.3402 0.4222 -0.0578 -0.0747 0.0370  144 SER A O   
979  C  CB  . SER A 144 ? 0.5042 0.4145 0.4947 -0.0495 -0.0685 0.0412  144 SER A CB  
980  O  OG  . SER A 144 ? 0.5500 0.4578 0.5435 -0.0516 -0.0692 0.0445  144 SER A OG  
981  N  N   . LEU A 145 ? 0.4123 0.3215 0.3981 -0.0522 -0.0737 0.0304  145 LEU A N   
982  C  CA  . LEU A 145 ? 0.4335 0.3396 0.4175 -0.0536 -0.0761 0.0269  145 LEU A CA  
983  C  C   . LEU A 145 ? 0.4388 0.3425 0.4189 -0.0495 -0.0762 0.0228  145 LEU A C   
984  O  O   . LEU A 145 ? 0.4232 0.3293 0.4021 -0.0466 -0.0747 0.0216  145 LEU A O   
985  C  CB  . LEU A 145 ? 0.4633 0.3718 0.4471 -0.0571 -0.0778 0.0244  145 LEU A CB  
986  C  CG  . LEU A 145 ? 0.4409 0.3531 0.4221 -0.0562 -0.0772 0.0198  145 LEU A CG  
987  C  CD1 . LEU A 145 ? 0.5170 0.4302 0.4974 -0.0599 -0.0790 0.0174  145 LEU A CD1 
988  C  CD2 . LEU A 145 ? 0.4609 0.3773 0.4433 -0.0556 -0.0749 0.0222  145 LEU A CD2 
989  N  N   . ALA A 146 ? 0.4321 0.3307 0.4104 -0.0493 -0.0780 0.0211  146 ALA A N   
990  C  CA  . ALA A 146 ? 0.4375 0.3335 0.4121 -0.0453 -0.0785 0.0170  146 ALA A CA  
991  C  C   . ALA A 146 ? 0.4536 0.3491 0.4264 -0.0468 -0.0804 0.0124  146 ALA A C   
992  O  O   . ALA A 146 ? 0.4476 0.3394 0.4205 -0.0498 -0.0820 0.0133  146 ALA A O   
993  C  CB  . ALA A 146 ? 0.4593 0.3482 0.4322 -0.0429 -0.0786 0.0193  146 ALA A CB  
994  N  N   . VAL A 147 ? 0.4650 0.3638 0.4360 -0.0445 -0.0803 0.0074  147 VAL A N   
995  C  CA  . VAL A 147 ? 0.4786 0.3777 0.4479 -0.0458 -0.0817 0.0028  147 VAL A CA  
996  C  C   . VAL A 147 ? 0.4748 0.3727 0.4412 -0.0410 -0.0821 -0.0018 147 VAL A C   
997  O  O   . VAL A 147 ? 0.4933 0.3941 0.4598 -0.0374 -0.0811 -0.0027 147 VAL A O   
998  C  CB  . VAL A 147 ? 0.5063 0.4124 0.4769 -0.0484 -0.0806 0.0015  147 VAL A CB  
999  C  CG1 . VAL A 147 ? 0.4863 0.3942 0.4547 -0.0488 -0.0812 -0.0040 147 VAL A CG1 
1000 C  CG2 . VAL A 147 ? 0.4796 0.3864 0.4525 -0.0531 -0.0807 0.0057  147 VAL A CG2 
1001 N  N   . SER A 148 ? 0.4849 0.3785 0.4486 -0.0407 -0.0838 -0.0049 148 SER A N   
1002 C  CA  . SER A 148 ? 0.4815 0.3743 0.4427 -0.0354 -0.0842 -0.0092 148 SER A CA  
1003 C  C   . SER A 148 ? 0.4906 0.3913 0.4525 -0.0345 -0.0833 -0.0143 148 SER A C   
1004 O  O   . SER A 148 ? 0.5069 0.4121 0.4700 -0.0384 -0.0826 -0.0151 148 SER A O   
1005 C  CB  . SER A 148 ? 0.5897 0.4745 0.5472 -0.0342 -0.0861 -0.0110 148 SER A CB  
1006 O  OG  . SER A 148 ? 0.6717 0.5494 0.6288 -0.0371 -0.0870 -0.0064 148 SER A OG  
1007 N  N   . LEU A 149 ? 0.4776 0.3803 0.4387 -0.0294 -0.0833 -0.0176 149 LEU A N   
1008 C  CA  . LEU A 149 ? 0.5051 0.4161 0.4674 -0.0283 -0.0824 -0.0226 149 LEU A CA  
1009 C  C   . LEU A 149 ? 0.5323 0.4438 0.4934 -0.0310 -0.0826 -0.0261 149 LEU A C   
1010 O  O   . LEU A 149 ? 0.5249 0.4298 0.4833 -0.0306 -0.0840 -0.0268 149 LEU A O   
1011 C  CB  . LEU A 149 ? 0.5115 0.4236 0.4730 -0.0219 -0.0830 -0.0261 149 LEU A CB  
1012 C  CG  . LEU A 149 ? 0.6166 0.5310 0.5792 -0.0189 -0.0826 -0.0242 149 LEU A CG  
1013 C  CD1 . LEU A 149 ? 0.6587 0.5742 0.6201 -0.0125 -0.0838 -0.0284 149 LEU A CD1 
1014 C  CD2 . LEU A 149 ? 0.6347 0.5574 0.6002 -0.0214 -0.0807 -0.0242 149 LEU A CD2 
1015 N  N   . GLY A 150 ? 0.4959 0.4147 0.4586 -0.0338 -0.0810 -0.0283 150 GLY A N   
1016 C  CA  . GLY A 150 ? 0.5088 0.4282 0.4699 -0.0363 -0.0809 -0.0318 150 GLY A CA  
1017 C  C   . GLY A 150 ? 0.4891 0.4048 0.4491 -0.0420 -0.0814 -0.0286 150 GLY A C   
1018 O  O   . GLY A 150 ? 0.5479 0.4649 0.5064 -0.0448 -0.0810 -0.0311 150 GLY A O   
1019 N  N   . GLN A 151 ? 0.4585 0.3699 0.4194 -0.0437 -0.0821 -0.0231 151 GLN A N   
1020 C  CA  . GLN A 151 ? 0.4608 0.3690 0.4212 -0.0489 -0.0830 -0.0200 151 GLN A CA  
1021 C  C   . GLN A 151 ? 0.4837 0.3974 0.4463 -0.0523 -0.0815 -0.0175 151 GLN A C   
1022 O  O   . GLN A 151 ? 0.4593 0.3788 0.4232 -0.0509 -0.0797 -0.0189 151 GLN A O   
1023 C  CB  . GLN A 151 ? 0.5032 0.4039 0.4636 -0.0488 -0.0846 -0.0156 151 GLN A CB  
1024 C  CG  . GLN A 151 ? 0.5610 0.4548 0.5181 -0.0459 -0.0862 -0.0179 151 GLN A CG  
1025 C  CD  . GLN A 151 ? 0.6429 0.5338 0.5967 -0.0484 -0.0874 -0.0210 151 GLN A CD  
1026 O  OE1 . GLN A 151 ? 0.6617 0.5549 0.6136 -0.0465 -0.0868 -0.0262 151 GLN A OE1 
1027 N  NE2 . GLN A 151 ? 0.6444 0.5307 0.5976 -0.0529 -0.0889 -0.0180 151 GLN A NE2 
1028 N  N   . ARG A 152 ? 0.4536 0.3653 0.4163 -0.0567 -0.0823 -0.0141 152 ARG A N   
1029 C  CA  . ARG A 152 ? 0.4091 0.3249 0.3731 -0.0600 -0.0811 -0.0118 152 ARG A CA  
1030 C  C   . ARG A 152 ? 0.4039 0.3189 0.3710 -0.0605 -0.0812 -0.0058 152 ARG A C   
1031 O  O   . ARG A 152 ? 0.4152 0.3255 0.3833 -0.0610 -0.0827 -0.0026 152 ARG A O   
1032 C  CB  . ARG A 152 ? 0.4434 0.3578 0.4051 -0.0645 -0.0823 -0.0122 152 ARG A CB  
1033 C  CG  . ARG A 152 ? 0.4555 0.3729 0.4176 -0.0681 -0.0816 -0.0095 152 ARG A CG  
1034 C  CD  . ARG A 152 ? 0.4690 0.3848 0.4275 -0.0719 -0.0828 -0.0112 152 ARG A CD  
1035 N  NE  . ARG A 152 ? 0.4429 0.3605 0.3981 -0.0714 -0.0814 -0.0170 152 ARG A NE  
1036 C  CZ  . ARG A 152 ? 0.4916 0.4140 0.4456 -0.0720 -0.0790 -0.0193 152 ARG A CZ  
1037 N  NH1 . ARG A 152 ? 0.4303 0.3556 0.3857 -0.0731 -0.0778 -0.0163 152 ARG A NH1 
1038 N  NH2 . ARG A 152 ? 0.5078 0.4320 0.4591 -0.0717 -0.0778 -0.0246 152 ARG A NH2 
1039 N  N   . ALA A 153 ? 0.3659 0.2853 0.3344 -0.0603 -0.0793 -0.0043 153 ALA A N   
1040 C  CA  . ALA A 153 ? 0.3823 0.3016 0.3534 -0.0613 -0.0789 0.0012  153 ALA A CA  
1041 C  C   . ALA A 153 ? 0.4162 0.3380 0.3869 -0.0650 -0.0786 0.0026  153 ALA A C   
1042 O  O   . ALA A 153 ? 0.4075 0.3325 0.3761 -0.0658 -0.0772 -0.0003 153 ALA A O   
1043 C  CB  . ALA A 153 ? 0.3880 0.3097 0.3603 -0.0578 -0.0770 0.0020  153 ALA A CB  
1044 N  N   . THR A 154 ? 0.3794 0.2998 0.3522 -0.0673 -0.0798 0.0072  154 THR A N   
1045 C  CA  . THR A 154 ? 0.3905 0.3127 0.3628 -0.0705 -0.0799 0.0090  154 THR A CA  
1046 C  C   . THR A 154 ? 0.3695 0.2925 0.3455 -0.0703 -0.0795 0.0148  154 THR A C   
1047 O  O   . THR A 154 ? 0.4173 0.3384 0.3965 -0.0700 -0.0805 0.0180  154 THR A O   
1048 C  CB  . THR A 154 ? 0.4013 0.3208 0.3721 -0.0739 -0.0826 0.0083  154 THR A CB  
1049 O  OG1 . THR A 154 ? 0.4266 0.3449 0.3938 -0.0738 -0.0829 0.0029  154 THR A OG1 
1050 C  CG2 . THR A 154 ? 0.3881 0.3090 0.3583 -0.0772 -0.0833 0.0106  154 THR A CG2 
1051 N  N   . ILE A 155 ? 0.3451 0.2708 0.3206 -0.0703 -0.0777 0.0162  155 ILE A N   
1052 C  CA  . ILE A 155 ? 0.3847 0.3115 0.3634 -0.0692 -0.0767 0.0214  155 ILE A CA  
1053 C  C   . ILE A 155 ? 0.3970 0.3252 0.3746 -0.0716 -0.0769 0.0233  155 ILE A C   
1054 O  O   . ILE A 155 ? 0.4145 0.3433 0.3880 -0.0726 -0.0760 0.0205  155 ILE A O   
1055 C  CB  . ILE A 155 ? 0.3843 0.3120 0.3625 -0.0657 -0.0740 0.0211  155 ILE A CB  
1056 C  CG1 . ILE A 155 ? 0.3856 0.3118 0.3641 -0.0629 -0.0739 0.0188  155 ILE A CG1 
1057 C  CG2 . ILE A 155 ? 0.3884 0.3170 0.3692 -0.0643 -0.0725 0.0263  155 ILE A CG2 
1058 C  CD1 . ILE A 155 ? 0.3884 0.3157 0.3658 -0.0595 -0.0716 0.0179  155 ILE A CD1 
1059 N  N   . SER A 156 ? 0.3500 0.2789 0.3314 -0.0723 -0.0780 0.0281  156 SER A N   
1060 C  CA  . SER A 156 ? 0.3728 0.3030 0.3537 -0.0741 -0.0786 0.0306  156 SER A CA  
1061 C  C   . SER A 156 ? 0.3782 0.3100 0.3604 -0.0716 -0.0762 0.0343  156 SER A C   
1062 O  O   . SER A 156 ? 0.3911 0.3234 0.3768 -0.0691 -0.0749 0.0369  156 SER A O   
1063 C  CB  . SER A 156 ? 0.4044 0.3348 0.3889 -0.0765 -0.0817 0.0334  156 SER A CB  
1064 O  OG  . SER A 156 ? 0.4126 0.3451 0.3981 -0.0775 -0.0826 0.0368  156 SER A OG  
1065 N  N   . CYS A 157 ? 0.3825 0.3145 0.3612 -0.0721 -0.0755 0.0346  157 CYS A N   
1066 C  CA  . CYS A 157 ? 0.3781 0.3110 0.3574 -0.0700 -0.0736 0.0384  157 CYS A CA  
1067 C  C   . CYS A 157 ? 0.4188 0.3523 0.3974 -0.0718 -0.0754 0.0408  157 CYS A C   
1068 O  O   . CYS A 157 ? 0.4289 0.3608 0.4023 -0.0739 -0.0761 0.0382  157 CYS A O   
1069 C  CB  . CYS A 157 ? 0.4259 0.3574 0.4000 -0.0686 -0.0707 0.0358  157 CYS A CB  
1070 S  SG  . CYS A 157 ? 0.4856 0.4168 0.4584 -0.0662 -0.0683 0.0401  157 CYS A SG  
1071 N  N   . LYS A 158 ? 0.3859 0.3217 0.3693 -0.0707 -0.0759 0.0458  158 LYS A N   
1072 C  CA  . LYS A 158 ? 0.3970 0.3338 0.3802 -0.0718 -0.0779 0.0484  158 LYS A CA  
1073 C  C   . LYS A 158 ? 0.4185 0.3562 0.4023 -0.0686 -0.0757 0.0524  158 LYS A C   
1074 O  O   . LYS A 158 ? 0.4204 0.3598 0.4088 -0.0660 -0.0739 0.0550  158 LYS A O   
1075 C  CB  . LYS A 158 ? 0.4110 0.3508 0.4007 -0.0737 -0.0813 0.0510  158 LYS A CB  
1076 C  CG  . LYS A 158 ? 0.4290 0.3670 0.4169 -0.0771 -0.0839 0.0470  158 LYS A CG  
1077 C  CD  . LYS A 158 ? 0.4639 0.4043 0.4576 -0.0795 -0.0875 0.0492  158 LYS A CD  
1078 C  CE  . LYS A 158 ? 0.5301 0.4677 0.5209 -0.0829 -0.0902 0.0452  158 LYS A CE  
1079 N  NZ  . LYS A 158 ? 0.5334 0.4729 0.5297 -0.0855 -0.0937 0.0472  158 LYS A NZ  
1080 N  N   . ALA A 159 ? 0.3886 0.3245 0.3672 -0.0687 -0.0758 0.0528  159 ALA A N   
1081 C  CA  . ALA A 159 ? 0.3802 0.3157 0.3577 -0.0654 -0.0736 0.0562  159 ALA A CA  
1082 C  C   . ALA A 159 ? 0.4326 0.3716 0.4146 -0.0649 -0.0761 0.0608  159 ALA A C   
1083 O  O   . ALA A 159 ? 0.4273 0.3670 0.4092 -0.0676 -0.0795 0.0603  159 ALA A O   
1084 C  CB  . ALA A 159 ? 0.3675 0.2981 0.3357 -0.0657 -0.0721 0.0538  159 ALA A CB  
1085 N  N   . SER A 160 ? 0.4312 0.3720 0.4162 -0.0612 -0.0744 0.0650  160 SER A N   
1086 C  CA  . SER A 160 ? 0.4325 0.3776 0.4225 -0.0601 -0.0765 0.0695  160 SER A CA  
1087 C  C   . SER A 160 ? 0.4716 0.4137 0.4549 -0.0603 -0.0782 0.0696  160 SER A C   
1088 O  O   . SER A 160 ? 0.4879 0.4333 0.4742 -0.0603 -0.0811 0.0725  160 SER A O   
1089 C  CB  . SER A 160 ? 0.4685 0.4167 0.4638 -0.0559 -0.0739 0.0738  160 SER A CB  
1090 O  OG  . SER A 160 ? 0.4426 0.3862 0.4316 -0.0527 -0.0703 0.0737  160 SER A OG  
1091 N  N   . GLN A 161 ? 0.4348 0.3707 0.4087 -0.0603 -0.0760 0.0669  161 GLN A N   
1092 C  CA  . GLN A 161 ? 0.4949 0.4264 0.4608 -0.0610 -0.0773 0.0665  161 GLN A CA  
1093 C  C   . GLN A 161 ? 0.4959 0.4219 0.4534 -0.0641 -0.0761 0.0612  161 GLN A C   
1094 O  O   . GLN A 161 ? 0.4578 0.3834 0.4156 -0.0646 -0.0737 0.0584  161 GLN A O   
1095 C  CB  . GLN A 161 ? 0.5234 0.4517 0.4849 -0.0569 -0.0749 0.0693  161 GLN A CB  
1096 C  CG  . GLN A 161 ? 0.6271 0.5608 0.5964 -0.0527 -0.0750 0.0747  161 GLN A CG  
1097 C  CD  . GLN A 161 ? 0.7167 0.6464 0.6814 -0.0481 -0.0715 0.0769  161 GLN A CD  
1098 O  OE1 . GLN A 161 ? 0.6941 0.6263 0.6636 -0.0447 -0.0689 0.0793  161 GLN A OE1 
1099 N  NE2 . GLN A 161 ? 0.7963 0.7192 0.7511 -0.0481 -0.0713 0.0761  161 GLN A NE2 
1100 N  N   . SER A 162 ? 0.4710 0.3928 0.4209 -0.0661 -0.0776 0.0600  162 SER A N   
1101 C  CA  . SER A 162 ? 0.5114 0.4283 0.4531 -0.0694 -0.0764 0.0550  162 SER A CA  
1102 C  C   . SER A 162 ? 0.5017 0.4147 0.4386 -0.0682 -0.0720 0.0533  162 SER A C   
1103 O  O   . SER A 162 ? 0.4895 0.4002 0.4242 -0.0650 -0.0701 0.0561  162 SER A O   
1104 C  CB  . SER A 162 ? 0.5149 0.4274 0.4485 -0.0712 -0.0783 0.0549  162 SER A CB  
1105 O  OG  . SER A 162 ? 0.5062 0.4139 0.4317 -0.0745 -0.0765 0.0501  162 SER A OG  
1106 N  N   . VAL A 163 ? 0.4536 0.3658 0.3884 -0.0707 -0.0704 0.0486  163 VAL A N   
1107 C  CA  . VAL A 163 ? 0.4603 0.3690 0.3903 -0.0702 -0.0666 0.0464  163 VAL A CA  
1108 C  C   . VAL A 163 ? 0.4978 0.4016 0.4185 -0.0739 -0.0656 0.0425  163 VAL A C   
1109 O  O   . VAL A 163 ? 0.5150 0.4169 0.4320 -0.0749 -0.0627 0.0393  163 VAL A O   
1110 C  CB  . VAL A 163 ? 0.4682 0.3806 0.4040 -0.0695 -0.0651 0.0444  163 VAL A CB  
1111 C  CG1 . VAL A 163 ? 0.4673 0.3840 0.4117 -0.0659 -0.0657 0.0486  163 VAL A CG1 
1112 C  CG2 . VAL A 163 ? 0.4693 0.3841 0.4069 -0.0729 -0.0666 0.0401  163 VAL A CG2 
1113 N  N   . ASP A 164 ? 0.4932 0.3950 0.4099 -0.0759 -0.0680 0.0428  164 ASP A N   
1114 C  CA  . ASP A 164 ? 0.4899 0.3869 0.3974 -0.0797 -0.0669 0.0391  164 ASP A CA  
1115 C  C   . ASP A 164 ? 0.5055 0.3953 0.4037 -0.0790 -0.0653 0.0410  164 ASP A C   
1116 O  O   . ASP A 164 ? 0.5095 0.3982 0.4081 -0.0759 -0.0664 0.0455  164 ASP A O   
1117 C  CB  . ASP A 164 ? 0.5442 0.4419 0.4507 -0.0829 -0.0698 0.0375  164 ASP A CB  
1118 C  CG  . ASP A 164 ? 0.5657 0.4685 0.4785 -0.0844 -0.0707 0.0341  164 ASP A CG  
1119 O  OD1 . ASP A 164 ? 0.5701 0.4762 0.4881 -0.0831 -0.0690 0.0329  164 ASP A OD1 
1120 O  OD2 . ASP A 164 ? 0.5903 0.4932 0.5019 -0.0870 -0.0730 0.0325  164 ASP A OD2 
1121 N  N   . TYR A 165 ? 0.4827 0.3677 0.3727 -0.0821 -0.0625 0.0375  165 TYR A N   
1122 C  CA  . TYR A 165 ? 0.5170 0.3939 0.3964 -0.0826 -0.0611 0.0386  165 TYR A CA  
1123 C  C   . TYR A 165 ? 0.5587 0.4321 0.4301 -0.0878 -0.0596 0.0341  165 TYR A C   
1124 O  O   . TYR A 165 ? 0.5000 0.3760 0.3727 -0.0902 -0.0574 0.0298  165 TYR A O   
1125 C  CB  . TYR A 165 ? 0.5134 0.3872 0.3909 -0.0801 -0.0579 0.0397  165 TYR A CB  
1126 C  CG  . TYR A 165 ? 0.5958 0.4600 0.4611 -0.0811 -0.0560 0.0403  165 TYR A CG  
1127 C  CD1 . TYR A 165 ? 0.5823 0.4419 0.4435 -0.0782 -0.0576 0.0448  165 TYR A CD1 
1128 C  CD2 . TYR A 165 ? 0.5730 0.4329 0.4310 -0.0851 -0.0527 0.0363  165 TYR A CD2 
1129 C  CE1 . TYR A 165 ? 0.5834 0.4332 0.4326 -0.0791 -0.0560 0.0454  165 TYR A CE1 
1130 C  CE2 . TYR A 165 ? 0.6204 0.4707 0.4665 -0.0866 -0.0509 0.0367  165 TYR A CE2 
1131 C  CZ  . TYR A 165 ? 0.6333 0.4781 0.4746 -0.0834 -0.0525 0.0414  165 TYR A CZ  
1132 O  OH  . TYR A 165 ? 0.6480 0.4824 0.4770 -0.0846 -0.0507 0.0419  165 TYR A OH  
1133 N  N   . ASP A 166 ? 0.5599 0.4274 0.4229 -0.0893 -0.0607 0.0351  166 ASP A N   
1134 C  CA  . ASP A 166 ? 0.5851 0.4482 0.4391 -0.0943 -0.0590 0.0312  166 ASP A CA  
1135 C  C   . ASP A 166 ? 0.5898 0.4591 0.4487 -0.0974 -0.0591 0.0266  166 ASP A C   
1136 O  O   . ASP A 166 ? 0.6601 0.5289 0.5154 -0.1011 -0.0561 0.0222  166 ASP A O   
1137 C  CB  . ASP A 166 ? 0.6266 0.4835 0.4727 -0.0958 -0.0547 0.0299  166 ASP A CB  
1138 C  CG  . ASP A 166 ? 0.7842 0.6355 0.6199 -0.1012 -0.0523 0.0263  166 ASP A CG  
1139 O  OD1 . ASP A 166 ? 0.7001 0.5477 0.5300 -0.1026 -0.0542 0.0272  166 ASP A OD1 
1140 O  OD2 . ASP A 166 ? 0.7273 0.5783 0.5608 -0.1042 -0.0487 0.0227  166 ASP A OD2 
1141 N  N   . GLY A 167 ? 0.5388 0.4142 0.4062 -0.0960 -0.0625 0.0273  167 GLY A N   
1142 C  CA  . GLY A 167 ? 0.6206 0.5009 0.4917 -0.0987 -0.0627 0.0229  167 GLY A CA  
1143 C  C   . GLY A 167 ? 0.6368 0.5233 0.5156 -0.0980 -0.0608 0.0200  167 GLY A C   
1144 O  O   . GLY A 167 ? 0.6619 0.5527 0.5442 -0.0996 -0.0609 0.0163  167 GLY A O   
1145 N  N   . ASP A 168 ? 0.5630 0.4495 0.4439 -0.0954 -0.0589 0.0216  168 ASP A N   
1146 C  CA  . ASP A 168 ? 0.5297 0.4216 0.4176 -0.0942 -0.0574 0.0193  168 ASP A CA  
1147 C  C   . ASP A 168 ? 0.5025 0.3981 0.3991 -0.0897 -0.0594 0.0232  168 ASP A C   
1148 O  O   . ASP A 168 ? 0.5016 0.3944 0.3973 -0.0871 -0.0602 0.0277  168 ASP A O   
1149 C  CB  . ASP A 168 ? 0.5324 0.4214 0.4160 -0.0946 -0.0537 0.0183  168 ASP A CB  
1150 C  CG  . ASP A 168 ? 0.6139 0.4992 0.4889 -0.0993 -0.0509 0.0144  168 ASP A CG  
1151 O  OD1 . ASP A 168 ? 0.6216 0.5098 0.4969 -0.1023 -0.0509 0.0106  168 ASP A OD1 
1152 O  OD2 . ASP A 168 ? 0.6627 0.5423 0.5308 -0.1001 -0.0486 0.0151  168 ASP A OD2 
1153 N  N   . SER A 169 ? 0.4723 0.3739 0.3770 -0.0886 -0.0601 0.0215  169 SER A N   
1154 C  CA  . SER A 169 ? 0.4412 0.3461 0.3539 -0.0847 -0.0615 0.0250  169 SER A CA  
1155 C  C   . SER A 169 ? 0.4129 0.3184 0.3271 -0.0825 -0.0588 0.0248  169 SER A C   
1156 O  O   . SER A 169 ? 0.5037 0.4112 0.4182 -0.0837 -0.0572 0.0206  169 SER A O   
1157 C  CB  . SER A 169 ? 0.4249 0.3350 0.3448 -0.0847 -0.0636 0.0234  169 SER A CB  
1158 O  OG  . SER A 169 ? 0.4591 0.3687 0.3782 -0.0865 -0.0665 0.0240  169 SER A OG  
1159 N  N   . TYR A 170 ? 0.4253 0.3285 0.3394 -0.0793 -0.0582 0.0291  170 TYR A N   
1160 C  CA  . TYR A 170 ? 0.4380 0.3409 0.3530 -0.0767 -0.0559 0.0296  170 TYR A CA  
1161 C  C   . TYR A 170 ? 0.4567 0.3648 0.3807 -0.0738 -0.0569 0.0306  170 TYR A C   
1162 O  O   . TYR A 170 ? 0.4066 0.3149 0.3338 -0.0702 -0.0566 0.0345  170 TYR A O   
1163 C  CB  . TYR A 170 ? 0.4206 0.3181 0.3308 -0.0743 -0.0546 0.0337  170 TYR A CB  
1164 C  CG  . TYR A 170 ? 0.4576 0.3489 0.3576 -0.0775 -0.0527 0.0315  170 TYR A CG  
1165 C  CD1 . TYR A 170 ? 0.4732 0.3622 0.3682 -0.0808 -0.0539 0.0306  170 TYR A CD1 
1166 C  CD2 . TYR A 170 ? 0.4817 0.3692 0.3766 -0.0776 -0.0496 0.0302  170 TYR A CD2 
1167 C  CE1 . TYR A 170 ? 0.4897 0.3726 0.3750 -0.0841 -0.0518 0.0285  170 TYR A CE1 
1168 C  CE2 . TYR A 170 ? 0.5023 0.3838 0.3876 -0.0811 -0.0477 0.0281  170 TYR A CE2 
1169 C  CZ  . TYR A 170 ? 0.5409 0.4201 0.4215 -0.0843 -0.0487 0.0273  170 TYR A CZ  
1170 O  OH  . TYR A 170 ? 0.5532 0.4261 0.4239 -0.0880 -0.0464 0.0253  170 TYR A OH  
1171 N  N   . MET A 171 ? 0.4133 0.3254 0.3410 -0.0753 -0.0577 0.0270  171 MET A N   
1172 C  CA  A MET A 171 ? 0.3796 0.2958 0.3149 -0.0727 -0.0584 0.0276  171 MET A CA  
1173 C  CA  B MET A 171 ? 0.4263 0.3428 0.3619 -0.0730 -0.0588 0.0274  171 MET A CA  
1174 C  C   . MET A 171 ? 0.4013 0.3201 0.3372 -0.0739 -0.0576 0.0224  171 MET A C   
1175 O  O   . MET A 171 ? 0.3966 0.3156 0.3293 -0.0771 -0.0575 0.0184  171 MET A O   
1176 C  CB  A MET A 171 ? 0.3435 0.2625 0.2849 -0.0722 -0.0615 0.0302  171 MET A CB  
1177 C  CB  B MET A 171 ? 0.4546 0.3733 0.3941 -0.0741 -0.0620 0.0286  171 MET A CB  
1178 C  CG  A MET A 171 ? 0.3213 0.2421 0.2634 -0.0752 -0.0635 0.0267  171 MET A CG  
1179 C  CG  B MET A 171 ? 0.5016 0.4239 0.4467 -0.0742 -0.0635 0.0264  171 MET A CG  
1180 S  SD  A MET A 171 ? 0.3550 0.2792 0.3011 -0.0748 -0.0633 0.0222  171 MET A SD  
1181 S  SD  B MET A 171 ? 0.5824 0.5071 0.5350 -0.0700 -0.0635 0.0299  171 MET A SD  
1182 C  CE  A MET A 171 ? 0.3869 0.3133 0.3409 -0.0710 -0.0642 0.0261  171 MET A CE  
1183 C  CE  B MET A 171 ? 0.4712 0.3947 0.4248 -0.0678 -0.0635 0.0364  171 MET A CE  
1184 N  N   . ASN A 172 ? 0.3598 0.2803 0.2993 -0.0710 -0.0568 0.0225  172 ASN A N   
1185 C  CA  . ASN A 172 ? 0.3542 0.2775 0.2949 -0.0711 -0.0562 0.0179  172 ASN A CA  
1186 C  C   . ASN A 172 ? 0.3621 0.2881 0.3094 -0.0683 -0.0577 0.0190  172 ASN A C   
1187 O  O   . ASN A 172 ? 0.3737 0.2992 0.3243 -0.0661 -0.0583 0.0235  172 ASN A O   
1188 C  CB  . ASN A 172 ? 0.3390 0.2609 0.2764 -0.0700 -0.0537 0.0169  172 ASN A CB  
1189 C  CG  . ASN A 172 ? 0.4093 0.3272 0.3394 -0.0726 -0.0519 0.0164  172 ASN A CG  
1190 O  OD1 . ASN A 172 ? 0.3719 0.2890 0.2988 -0.0760 -0.0521 0.0148  172 ASN A OD1 
1191 N  ND2 . ASN A 172 ? 0.3721 0.2868 0.2986 -0.0713 -0.0499 0.0175  172 ASN A ND2 
1192 N  N   . TRP A 173 ? 0.3556 0.2845 0.3048 -0.0684 -0.0580 0.0148  173 TRP A N   
1193 C  CA  . TRP A 173 ? 0.3567 0.2873 0.3109 -0.0654 -0.0591 0.0151  173 TRP A CA  
1194 C  C   . TRP A 173 ? 0.3857 0.3174 0.3391 -0.0634 -0.0576 0.0126  173 TRP A C   
1195 O  O   . TRP A 173 ? 0.3787 0.3117 0.3291 -0.0652 -0.0565 0.0085  173 TRP A O   
1196 C  CB  . TRP A 173 ? 0.3796 0.3124 0.3362 -0.0667 -0.0610 0.0120  173 TRP A CB  
1197 C  CG  . TRP A 173 ? 0.3420 0.2738 0.2999 -0.0685 -0.0631 0.0144  173 TRP A CG  
1198 C  CD1 . TRP A 173 ? 0.3739 0.3051 0.3288 -0.0719 -0.0637 0.0131  173 TRP A CD1 
1199 C  CD2 . TRP A 173 ? 0.3468 0.2781 0.3093 -0.0672 -0.0649 0.0181  173 TRP A CD2 
1200 N  NE1 . TRP A 173 ? 0.3781 0.3085 0.3353 -0.0726 -0.0661 0.0159  173 TRP A NE1 
1201 C  CE2 . TRP A 173 ? 0.3738 0.3046 0.3360 -0.0699 -0.0668 0.0190  173 TRP A CE2 
1202 C  CE3 . TRP A 173 ? 0.3402 0.2715 0.3068 -0.0641 -0.0649 0.0209  173 TRP A CE3 
1203 C  CZ2 . TRP A 173 ? 0.4060 0.3366 0.3724 -0.0700 -0.0690 0.0223  173 TRP A CZ2 
1204 C  CZ3 . TRP A 173 ? 0.3624 0.2934 0.3330 -0.0642 -0.0668 0.0243  173 TRP A CZ3 
1205 C  CH2 . TRP A 173 ? 0.3855 0.3164 0.3563 -0.0672 -0.0689 0.0249  173 TRP A CH2 
1206 N  N   . TYR A 174 ? 0.3634 0.2944 0.3194 -0.0599 -0.0576 0.0152  174 TYR A N   
1207 C  CA  . TYR A 174 ? 0.3516 0.2832 0.3070 -0.0574 -0.0567 0.0133  174 TYR A CA  
1208 C  C   . TYR A 174 ? 0.3454 0.2786 0.3049 -0.0550 -0.0583 0.0124  174 TYR A C   
1209 O  O   . TYR A 174 ? 0.3511 0.2834 0.3138 -0.0545 -0.0596 0.0152  174 TYR A O   
1210 C  CB  . TYR A 174 ? 0.3448 0.2733 0.2984 -0.0550 -0.0549 0.0174  174 TYR A CB  
1211 C  CG  . TYR A 174 ? 0.3582 0.2845 0.3068 -0.0572 -0.0533 0.0176  174 TYR A CG  
1212 C  CD1 . TYR A 174 ? 0.3637 0.2899 0.3079 -0.0584 -0.0519 0.0140  174 TYR A CD1 
1213 C  CD2 . TYR A 174 ? 0.3602 0.2844 0.3082 -0.0582 -0.0532 0.0213  174 TYR A CD2 
1214 C  CE1 . TYR A 174 ? 0.3889 0.3122 0.3278 -0.0609 -0.0503 0.0140  174 TYR A CE1 
1215 C  CE2 . TYR A 174 ? 0.4010 0.3223 0.3435 -0.0601 -0.0517 0.0215  174 TYR A CE2 
1216 C  CZ  . TYR A 174 ? 0.3972 0.3177 0.3350 -0.0616 -0.0502 0.0179  174 TYR A CZ  
1217 O  OH  . TYR A 174 ? 0.3814 0.2982 0.3133 -0.0639 -0.0488 0.0181  174 TYR A OH  
1218 N  N   . GLN A 175 ? 0.3628 0.2980 0.3218 -0.0535 -0.0584 0.0085  175 GLN A N   
1219 C  CA  . GLN A 175 ? 0.3788 0.3145 0.3406 -0.0504 -0.0598 0.0077  175 GLN A CA  
1220 C  C   . GLN A 175 ? 0.3637 0.2983 0.3241 -0.0469 -0.0590 0.0084  175 GLN A C   
1221 O  O   . GLN A 175 ? 0.3751 0.3106 0.3325 -0.0473 -0.0579 0.0061  175 GLN A O   
1222 C  CB  . GLN A 175 ? 0.3725 0.3122 0.3348 -0.0514 -0.0609 0.0019  175 GLN A CB  
1223 C  CG  . GLN A 175 ? 0.3685 0.3089 0.3331 -0.0480 -0.0625 0.0001  175 GLN A CG  
1224 C  CD  . GLN A 175 ? 0.4000 0.3450 0.3649 -0.0484 -0.0632 -0.0059 175 GLN A CD  
1225 O  OE1 . GLN A 175 ? 0.4034 0.3520 0.3670 -0.0493 -0.0623 -0.0092 175 GLN A OE1 
1226 N  NE2 . GLN A 175 ? 0.3791 0.3244 0.3460 -0.0478 -0.0648 -0.0075 175 GLN A NE2 
1227 N  N   . GLN A 176 ? 0.3487 0.2810 0.3108 -0.0438 -0.0596 0.0112  176 GLN A N   
1228 C  CA  . GLN A 176 ? 0.3582 0.2891 0.3186 -0.0401 -0.0591 0.0115  176 GLN A CA  
1229 C  C   . GLN A 176 ? 0.3485 0.2794 0.3106 -0.0372 -0.0610 0.0099  176 GLN A C   
1230 O  O   . GLN A 176 ? 0.3733 0.3015 0.3374 -0.0361 -0.0615 0.0130  176 GLN A O   
1231 C  CB  . GLN A 176 ? 0.3587 0.2855 0.3181 -0.0383 -0.0574 0.0170  176 GLN A CB  
1232 C  CG  . GLN A 176 ? 0.4049 0.3298 0.3614 -0.0345 -0.0568 0.0170  176 GLN A CG  
1233 C  CD  . GLN A 176 ? 0.4072 0.3282 0.3617 -0.0328 -0.0546 0.0219  176 GLN A CD  
1234 O  OE1 . GLN A 176 ? 0.4088 0.3284 0.3656 -0.0332 -0.0537 0.0263  176 GLN A OE1 
1235 N  NE2 . GLN A 176 ? 0.3947 0.3143 0.3448 -0.0311 -0.0536 0.0209  176 GLN A NE2 
1236 N  N   . LYS A 177 ? 0.3827 0.3169 0.3442 -0.0362 -0.0620 0.0048  177 LYS A N   
1237 C  CA  . LYS A 177 ? 0.3891 0.3230 0.3515 -0.0328 -0.0639 0.0031  177 LYS A CA  
1238 C  C   . LYS A 177 ? 0.4303 0.3602 0.3905 -0.0288 -0.0636 0.0061  177 LYS A C   
1239 O  O   . LYS A 177 ? 0.4062 0.3349 0.3638 -0.0285 -0.0620 0.0077  177 LYS A O   
1240 C  CB  . LYS A 177 ? 0.4106 0.3499 0.3730 -0.0325 -0.0650 -0.0030 177 LYS A CB  
1241 C  CG  . LYS A 177 ? 0.4084 0.3515 0.3728 -0.0361 -0.0653 -0.0062 177 LYS A CG  
1242 C  CD  . LYS A 177 ? 0.4715 0.4209 0.4366 -0.0357 -0.0661 -0.0123 177 LYS A CD  
1243 C  CE  . LYS A 177 ? 0.4879 0.4410 0.4546 -0.0393 -0.0660 -0.0156 177 LYS A CE  
1244 N  NZ  . LYS A 177 ? 0.5345 0.4945 0.5023 -0.0389 -0.0664 -0.0215 177 LYS A NZ  
1245 N  N   . PRO A 178 ? 0.4277 0.3546 0.3881 -0.0255 -0.0649 0.0069  178 PRO A N   
1246 C  CA  . PRO A 178 ? 0.4348 0.3572 0.3926 -0.0216 -0.0644 0.0099  178 PRO A CA  
1247 C  C   . PRO A 178 ? 0.4521 0.3761 0.4065 -0.0195 -0.0645 0.0073  178 PRO A C   
1248 O  O   . PRO A 178 ? 0.4385 0.3670 0.3932 -0.0190 -0.0661 0.0023  178 PRO A O   
1249 C  CB  . PRO A 178 ? 0.4660 0.3853 0.4243 -0.0189 -0.0663 0.0099  178 PRO A CB  
1250 C  CG  . PRO A 178 ? 0.4761 0.3969 0.4379 -0.0224 -0.0670 0.0092  178 PRO A CG  
1251 C  CD  . PRO A 178 ? 0.4601 0.3872 0.4228 -0.0253 -0.0669 0.0049  178 PRO A CD  
1252 N  N   . GLY A 179 ? 0.4489 0.3697 0.4003 -0.0188 -0.0625 0.0107  179 GLY A N   
1253 C  CA  . GLY A 179 ? 0.4989 0.4198 0.4462 -0.0167 -0.0625 0.0090  179 GLY A CA  
1254 C  C   . GLY A 179 ? 0.4849 0.4104 0.4318 -0.0201 -0.0619 0.0057  179 GLY A C   
1255 O  O   . GLY A 179 ? 0.4806 0.4065 0.4241 -0.0191 -0.0621 0.0037  179 GLY A O   
1256 N  N   . GLN A 180 ? 0.4503 0.3785 0.4000 -0.0243 -0.0613 0.0051  180 GLN A N   
1257 C  CA  A GLN A 180 ? 0.4313 0.3636 0.3804 -0.0279 -0.0607 0.0017  180 GLN A CA  
1258 C  CA  B GLN A 180 ? 0.4348 0.3671 0.3839 -0.0279 -0.0607 0.0017  180 GLN A CA  
1259 C  C   . GLN A 180 ? 0.4398 0.3692 0.3874 -0.0307 -0.0582 0.0054  180 GLN A C   
1260 O  O   . GLN A 180 ? 0.3999 0.3260 0.3488 -0.0304 -0.0572 0.0100  180 GLN A O   
1261 C  CB  A GLN A 180 ? 0.4707 0.4087 0.4236 -0.0307 -0.0619 -0.0024 180 GLN A CB  
1262 C  CB  B GLN A 180 ? 0.4485 0.3867 0.4015 -0.0300 -0.0623 -0.0028 180 GLN A CB  
1263 C  CG  A GLN A 180 ? 0.5806 0.5232 0.5353 -0.0284 -0.0643 -0.0073 180 GLN A CG  
1264 C  CG  B GLN A 180 ? 0.4748 0.4153 0.4293 -0.0264 -0.0648 -0.0060 180 GLN A CG  
1265 C  CD  A GLN A 180 ? 0.5842 0.5294 0.5365 -0.0268 -0.0651 -0.0106 180 GLN A CD  
1266 C  CD  B GLN A 180 ? 0.4898 0.4371 0.4475 -0.0281 -0.0661 -0.0116 180 GLN A CD  
1267 O  OE1 A GLN A 180 ? 0.6925 0.6359 0.6433 -0.0225 -0.0665 -0.0104 180 GLN A OE1 
1268 O  OE1 B GLN A 180 ? 0.4753 0.4265 0.4336 -0.0322 -0.0650 -0.0139 180 GLN A OE1 
1269 N  NE2 A GLN A 180 ? 0.6920 0.6413 0.6437 -0.0304 -0.0643 -0.0138 180 GLN A NE2 
1270 N  NE2 B GLN A 180 ? 0.4849 0.4338 0.4445 -0.0248 -0.0683 -0.0138 180 GLN A NE2 
1271 N  N   . PRO A 181 ? 0.4178 0.3481 0.3626 -0.0334 -0.0570 0.0037  181 PRO A N   
1272 C  CA  . PRO A 181 ? 0.4303 0.3576 0.3735 -0.0359 -0.0547 0.0072  181 PRO A CA  
1273 C  C   . PRO A 181 ? 0.4090 0.3383 0.3558 -0.0391 -0.0549 0.0075  181 PRO A C   
1274 O  O   . PRO A 181 ? 0.4010 0.3347 0.3506 -0.0405 -0.0564 0.0038  181 PRO A O   
1275 C  CB  . PRO A 181 ? 0.4318 0.3593 0.3705 -0.0382 -0.0538 0.0043  181 PRO A CB  
1276 C  CG  . PRO A 181 ? 0.4677 0.3982 0.4057 -0.0361 -0.0556 0.0001  181 PRO A CG  
1277 C  CD  . PRO A 181 ? 0.4465 0.3808 0.3896 -0.0345 -0.0578 -0.0014 181 PRO A CD  
1278 N  N   . PRO A 182 ? 0.3920 0.3185 0.3387 -0.0405 -0.0535 0.0116  182 PRO A N   
1279 C  CA  . PRO A 182 ? 0.3755 0.3039 0.3246 -0.0440 -0.0538 0.0114  182 PRO A CA  
1280 C  C   . PRO A 182 ? 0.3544 0.2857 0.3013 -0.0478 -0.0536 0.0066  182 PRO A C   
1281 O  O   . PRO A 182 ? 0.3662 0.2970 0.3093 -0.0482 -0.0527 0.0047  182 PRO A O   
1282 C  CB  . PRO A 182 ? 0.3733 0.2979 0.3214 -0.0443 -0.0522 0.0167  182 PRO A CB  
1283 C  CG  . PRO A 182 ? 0.4152 0.3361 0.3619 -0.0401 -0.0510 0.0203  182 PRO A CG  
1284 C  CD  . PRO A 182 ? 0.4219 0.3434 0.3657 -0.0386 -0.0514 0.0164  182 PRO A CD  
1285 N  N   . ARG A 183 ? 0.3548 0.2891 0.3040 -0.0507 -0.0545 0.0045  183 ARG A N   
1286 C  CA  . ARG A 183 ? 0.3593 0.2962 0.3064 -0.0547 -0.0538 0.0004  183 ARG A CA  
1287 C  C   . ARG A 183 ? 0.3713 0.3079 0.3189 -0.0579 -0.0538 0.0014  183 ARG A C   
1288 O  O   . ARG A 183 ? 0.3216 0.2581 0.2726 -0.0570 -0.0551 0.0033  183 ARG A O   
1289 C  CB  . ARG A 183 ? 0.3735 0.3161 0.3224 -0.0548 -0.0549 -0.0053 183 ARG A CB  
1290 C  CG  . ARG A 183 ? 0.3824 0.3281 0.3358 -0.0543 -0.0567 -0.0068 183 ARG A CG  
1291 C  CD  . ARG A 183 ? 0.3990 0.3506 0.3545 -0.0533 -0.0579 -0.0125 183 ARG A CD  
1292 N  NE  . ARG A 183 ? 0.4090 0.3626 0.3682 -0.0521 -0.0596 -0.0139 183 ARG A NE  
1293 C  CZ  . ARG A 183 ? 0.4016 0.3609 0.3628 -0.0528 -0.0601 -0.0190 183 ARG A CZ  
1294 N  NH1 . ARG A 183 ? 0.4238 0.3879 0.3844 -0.0547 -0.0593 -0.0232 183 ARG A NH1 
1295 N  NH2 . ARG A 183 ? 0.4231 0.3830 0.3868 -0.0518 -0.0615 -0.0199 183 ARG A NH2 
1296 N  N   . LEU A 184 ? 0.3713 0.3079 0.3154 -0.0618 -0.0525 -0.0004 184 LEU A N   
1297 C  CA  . LEU A 184 ? 0.3583 0.2945 0.3020 -0.0650 -0.0526 -0.0001 184 LEU A CA  
1298 C  C   . LEU A 184 ? 0.3478 0.2888 0.2952 -0.0659 -0.0541 -0.0039 184 LEU A C   
1299 O  O   . LEU A 184 ? 0.3646 0.3099 0.3129 -0.0661 -0.0541 -0.0086 184 LEU A O   
1300 C  CB  . LEU A 184 ? 0.3585 0.2933 0.2967 -0.0691 -0.0506 -0.0018 184 LEU A CB  
1301 C  CG  . LEU A 184 ? 0.3540 0.2879 0.2907 -0.0727 -0.0506 -0.0017 184 LEU A CG  
1302 C  CD1 . LEU A 184 ? 0.3838 0.3131 0.3199 -0.0718 -0.0511 0.0039  184 LEU A CD1 
1303 C  CD2 . LEU A 184 ? 0.3506 0.2836 0.2814 -0.0770 -0.0484 -0.0046 184 LEU A CD2 
1304 N  N   . LEU A 185 ? 0.3341 0.2742 0.2836 -0.0661 -0.0554 -0.0019 185 LEU A N   
1305 C  CA  . LEU A 185 ? 0.3497 0.2930 0.3018 -0.0669 -0.0568 -0.0052 185 LEU A CA  
1306 C  C   . LEU A 185 ? 0.3538 0.2966 0.3030 -0.0711 -0.0563 -0.0064 185 LEU A C   
1307 O  O   . LEU A 185 ? 0.3963 0.3427 0.3452 -0.0733 -0.0559 -0.0110 185 LEU A O   
1308 C  CB  . LEU A 185 ? 0.3450 0.2868 0.3010 -0.0640 -0.0589 -0.0021 185 LEU A CB  
1309 C  CG  . LEU A 185 ? 0.3467 0.2907 0.3053 -0.0639 -0.0606 -0.0052 185 LEU A CG  
1310 C  CD1 . LEU A 185 ? 0.3353 0.2829 0.2959 -0.0608 -0.0609 -0.0090 185 LEU A CD1 
1311 C  CD2 . LEU A 185 ? 0.3456 0.2865 0.3069 -0.0625 -0.0625 -0.0012 185 LEU A CD2 
1312 N  N   . ILE A 186 ? 0.3374 0.2761 0.2846 -0.0724 -0.0564 -0.0021 186 ILE A N   
1313 C  CA  . ILE A 186 ? 0.3747 0.3122 0.3186 -0.0762 -0.0563 -0.0028 186 ILE A CA  
1314 C  C   . ILE A 186 ? 0.3865 0.3194 0.3259 -0.0773 -0.0550 0.0009  186 ILE A C   
1315 O  O   . ILE A 186 ? 0.3565 0.2871 0.2972 -0.0747 -0.0555 0.0054  186 ILE A O   
1316 C  CB  . ILE A 186 ? 0.3888 0.3257 0.3354 -0.0760 -0.0587 -0.0013 186 ILE A CB  
1317 C  CG1 . ILE A 186 ? 0.4260 0.3666 0.3759 -0.0749 -0.0597 -0.0055 186 ILE A CG1 
1318 C  CG2 . ILE A 186 ? 0.3821 0.3166 0.3247 -0.0796 -0.0590 -0.0007 186 ILE A CG2 
1319 C  CD1 . ILE A 186 ? 0.4638 0.4032 0.4153 -0.0753 -0.0621 -0.0049 186 ILE A CD1 
1320 N  N   . TYR A 187 ? 0.3813 0.3128 0.3152 -0.0810 -0.0534 -0.0008 187 TYR A N   
1321 C  CA  . TYR A 187 ? 0.3943 0.3205 0.3233 -0.0817 -0.0524 0.0029  187 TYR A CA  
1322 C  C   . TYR A 187 ? 0.3911 0.3146 0.3165 -0.0846 -0.0532 0.0039  187 TYR A C   
1323 O  O   . TYR A 187 ? 0.3839 0.3093 0.3088 -0.0870 -0.0535 0.0005  187 TYR A O   
1324 C  CB  . TYR A 187 ? 0.4042 0.3290 0.3282 -0.0835 -0.0497 0.0008  187 TYR A CB  
1325 C  CG  . TYR A 187 ? 0.3961 0.3232 0.3171 -0.0878 -0.0482 -0.0045 187 TYR A CG  
1326 C  CD1 . TYR A 187 ? 0.4353 0.3686 0.3603 -0.0877 -0.0480 -0.0092 187 TYR A CD1 
1327 C  CD2 . TYR A 187 ? 0.4107 0.3340 0.3251 -0.0918 -0.0468 -0.0047 187 TYR A CD2 
1328 C  CE1 . TYR A 187 ? 0.4726 0.4091 0.3956 -0.0916 -0.0463 -0.0142 187 TYR A CE1 
1329 C  CE2 . TYR A 187 ? 0.4079 0.3336 0.3196 -0.0959 -0.0449 -0.0096 187 TYR A CE2 
1330 C  CZ  . TYR A 187 ? 0.4478 0.3804 0.3642 -0.0959 -0.0445 -0.0143 187 TYR A CZ  
1331 O  OH  . TYR A 187 ? 0.4936 0.4296 0.4081 -0.1000 -0.0425 -0.0193 187 TYR A OH  
1332 N  N   . ALA A 188 ? 0.3889 0.3078 0.3117 -0.0838 -0.0536 0.0086  188 ALA A N   
1333 C  CA  . ALA A 188 ? 0.4092 0.3248 0.3280 -0.0860 -0.0546 0.0103  188 ALA A CA  
1334 C  C   . ALA A 188 ? 0.4135 0.3320 0.3360 -0.0867 -0.0571 0.0090  188 ALA A C   
1335 O  O   . ALA A 188 ? 0.4100 0.3277 0.3287 -0.0899 -0.0572 0.0066  188 ALA A O   
1336 C  CB  . ALA A 188 ? 0.4213 0.3335 0.3318 -0.0901 -0.0523 0.0077  188 ALA A CB  
1337 N  N   . ALA A 189 ? 0.3843 0.3055 0.3137 -0.0837 -0.0590 0.0108  189 ALA A N   
1338 C  CA  . ALA A 189 ? 0.3842 0.3073 0.3178 -0.0837 -0.0618 0.0107  189 ALA A CA  
1339 C  C   . ALA A 189 ? 0.4005 0.3266 0.3350 -0.0850 -0.0617 0.0054  189 ALA A C   
1340 O  O   . ALA A 189 ? 0.4231 0.3514 0.3625 -0.0834 -0.0634 0.0048  189 ALA A O   
1341 C  CB  . ALA A 189 ? 0.3721 0.2923 0.3030 -0.0852 -0.0638 0.0137  189 ALA A CB  
1342 N  N   . SER A 190 ? 0.4060 0.3324 0.3359 -0.0877 -0.0596 0.0013  190 SER A N   
1343 C  CA  . SER A 190 ? 0.3849 0.3142 0.3156 -0.0890 -0.0599 -0.0034 190 SER A CA  
1344 C  C   . SER A 190 ? 0.4090 0.3418 0.3390 -0.0899 -0.0571 -0.0084 190 SER A C   
1345 O  O   . SER A 190 ? 0.4565 0.3924 0.3871 -0.0908 -0.0568 -0.0127 190 SER A O   
1346 C  CB  . SER A 190 ? 0.4701 0.3968 0.3961 -0.0922 -0.0607 -0.0040 190 SER A CB  
1347 O  OG  . SER A 190 ? 0.4727 0.3966 0.3919 -0.0951 -0.0584 -0.0044 190 SER A OG  
1348 N  N   . ASN A 191 ? 0.3765 0.3091 0.3049 -0.0899 -0.0549 -0.0080 191 ASN A N   
1349 C  CA  . ASN A 191 ? 0.3909 0.3275 0.3189 -0.0912 -0.0525 -0.0129 191 ASN A CA  
1350 C  C   . ASN A 191 ? 0.3997 0.3405 0.3334 -0.0876 -0.0528 -0.0141 191 ASN A C   
1351 O  O   . ASN A 191 ? 0.4136 0.3528 0.3484 -0.0851 -0.0529 -0.0108 191 ASN A O   
1352 C  CB  . ASN A 191 ? 0.3964 0.3297 0.3182 -0.0940 -0.0499 -0.0123 191 ASN A CB  
1353 C  CG  . ASN A 191 ? 0.4742 0.4025 0.3893 -0.0973 -0.0496 -0.0110 191 ASN A CG  
1354 O  OD1 . ASN A 191 ? 0.5352 0.4644 0.4474 -0.1005 -0.0485 -0.0145 191 ASN A OD1 
1355 N  ND2 . ASN A 191 ? 0.4792 0.4023 0.3920 -0.0963 -0.0508 -0.0059 191 ASN A ND2 
1356 N  N   . LEU A 192 ? 0.4065 0.3529 0.3431 -0.0874 -0.0524 -0.0190 192 LEU A N   
1357 C  CA  . LEU A 192 ? 0.4460 0.3964 0.3875 -0.0839 -0.0528 -0.0205 192 LEU A CA  
1358 C  C   . LEU A 192 ? 0.4565 0.4081 0.3962 -0.0848 -0.0507 -0.0215 192 LEU A C   
1359 O  O   . LEU A 192 ? 0.4470 0.3999 0.3834 -0.0887 -0.0485 -0.0245 192 LEU A O   
1360 C  CB  . LEU A 192 ? 0.4506 0.4069 0.3958 -0.0829 -0.0532 -0.0256 192 LEU A CB  
1361 C  CG  . LEU A 192 ? 0.5423 0.4974 0.4895 -0.0813 -0.0555 -0.0252 192 LEU A CG  
1362 C  CD1 . LEU A 192 ? 0.5662 0.5269 0.5173 -0.0788 -0.0558 -0.0300 192 LEU A CD1 
1363 C  CD2 . LEU A 192 ? 0.5889 0.5399 0.5381 -0.0783 -0.0576 -0.0199 192 LEU A CD2 
1364 N  N   . GLU A 193 ? 0.4392 0.3899 0.3808 -0.0816 -0.0513 -0.0191 193 GLU A N   
1365 C  CA  . GLU A 193 ? 0.4254 0.3774 0.3654 -0.0822 -0.0496 -0.0206 193 GLU A CA  
1366 C  C   . GLU A 193 ? 0.4292 0.3889 0.3724 -0.0826 -0.0492 -0.0267 193 GLU A C   
1367 O  O   . GLU A 193 ? 0.4175 0.3810 0.3649 -0.0805 -0.0506 -0.0288 193 GLU A O   
1368 C  CB  . GLU A 193 ? 0.4268 0.3759 0.3680 -0.0781 -0.0506 -0.0167 193 GLU A CB  
1369 C  CG  . GLU A 193 ? 0.4400 0.3913 0.3810 -0.0771 -0.0498 -0.0186 193 GLU A CG  
1370 C  CD  . GLU A 193 ? 0.5220 0.4705 0.4571 -0.0811 -0.0474 -0.0190 193 GLU A CD  
1371 O  OE1 . GLU A 193 ? 0.5335 0.4815 0.4654 -0.0854 -0.0460 -0.0204 193 GLU A OE1 
1372 O  OE2 . GLU A 193 ? 0.4983 0.4446 0.4314 -0.0800 -0.0469 -0.0179 193 GLU A OE2 
1373 N  N   . SER A 194 ? 0.4187 0.3808 0.3599 -0.0854 -0.0472 -0.0296 194 SER A N   
1374 C  CA  . SER A 194 ? 0.4593 0.4298 0.4041 -0.0858 -0.0468 -0.0353 194 SER A CA  
1375 C  C   . SER A 194 ? 0.4494 0.4235 0.3997 -0.0803 -0.0492 -0.0359 194 SER A C   
1376 O  O   . SER A 194 ? 0.4407 0.4110 0.3908 -0.0771 -0.0504 -0.0324 194 SER A O   
1377 C  CB  . SER A 194 ? 0.5202 0.4921 0.4623 -0.0890 -0.0448 -0.0374 194 SER A CB  
1378 O  OG  . SER A 194 ? 0.6679 0.6353 0.6040 -0.0940 -0.0425 -0.0366 194 SER A OG  
1379 N  N   . GLY A 195 ? 0.4791 0.4600 0.4339 -0.0791 -0.0498 -0.0402 195 GLY A N   
1380 C  CA  . GLY A 195 ? 0.4473 0.4320 0.4070 -0.0739 -0.0522 -0.0414 195 GLY A CA  
1381 C  C   . GLY A 195 ? 0.4891 0.4694 0.4503 -0.0698 -0.0544 -0.0381 195 GLY A C   
1382 O  O   . GLY A 195 ? 0.5278 0.5102 0.4924 -0.0653 -0.0563 -0.0389 195 GLY A O   
1383 N  N   . ILE A 196 ? 0.4472 0.4211 0.4055 -0.0714 -0.0542 -0.0341 196 ILE A N   
1384 C  CA  . ILE A 196 ? 0.4257 0.3957 0.3856 -0.0683 -0.0564 -0.0312 196 ILE A CA  
1385 C  C   . ILE A 196 ? 0.4752 0.4484 0.4369 -0.0684 -0.0568 -0.0349 196 ILE A C   
1386 O  O   . ILE A 196 ? 0.4835 0.4582 0.4432 -0.0723 -0.0552 -0.0371 196 ILE A O   
1387 C  CB  . ILE A 196 ? 0.4074 0.3701 0.3642 -0.0698 -0.0564 -0.0255 196 ILE A CB  
1388 C  CG1 . ILE A 196 ? 0.4051 0.3643 0.3600 -0.0690 -0.0558 -0.0216 196 ILE A CG1 
1389 C  CG2 . ILE A 196 ? 0.3830 0.3423 0.3417 -0.0675 -0.0586 -0.0228 196 ILE A CG2 
1390 C  CD1 . ILE A 196 ? 0.4158 0.3757 0.3732 -0.0643 -0.0570 -0.0210 196 ILE A CD1 
1391 N  N   . PRO A 197 ? 0.4331 0.4068 0.3979 -0.0641 -0.0589 -0.0356 197 PRO A N   
1392 C  CA  . PRO A 197 ? 0.4594 0.4355 0.4255 -0.0637 -0.0594 -0.0392 197 PRO A CA  
1393 C  C   . PRO A 197 ? 0.4902 0.4615 0.4534 -0.0667 -0.0593 -0.0375 197 PRO A C   
1394 O  O   . PRO A 197 ? 0.4515 0.4168 0.4129 -0.0675 -0.0601 -0.0326 197 PRO A O   
1395 C  CB  . PRO A 197 ? 0.4645 0.4401 0.4336 -0.0580 -0.0618 -0.0393 197 PRO A CB  
1396 C  CG  . PRO A 197 ? 0.5512 0.5249 0.5208 -0.0555 -0.0626 -0.0360 197 PRO A CG  
1397 C  CD  . PRO A 197 ? 0.4775 0.4490 0.4442 -0.0594 -0.0608 -0.0330 197 PRO A CD  
1398 N  N   . ALA A 198 ? 0.5024 0.4766 0.4654 -0.0679 -0.0587 -0.0416 198 ALA A N   
1399 C  CA  . ALA A 198 ? 0.5017 0.4719 0.4612 -0.0711 -0.0585 -0.0409 198 ALA A CA  
1400 C  C   . ALA A 198 ? 0.4757 0.4395 0.4352 -0.0690 -0.0613 -0.0375 198 ALA A C   
1401 O  O   . ALA A 198 ? 0.4983 0.4578 0.4549 -0.0717 -0.0617 -0.0357 198 ALA A O   
1402 C  CB  . ALA A 198 ? 0.6049 0.5797 0.5640 -0.0725 -0.0569 -0.0464 198 ALA A CB  
1403 N  N   . ARG A 199 ? 0.4615 0.4245 0.4241 -0.0645 -0.0632 -0.0366 199 ARG A N   
1404 C  CA  . ARG A 199 ? 0.4285 0.3851 0.3910 -0.0630 -0.0656 -0.0332 199 ARG A CA  
1405 C  C   . ARG A 199 ? 0.4609 0.4126 0.4223 -0.0650 -0.0662 -0.0272 199 ARG A C   
1406 O  O   . ARG A 199 ? 0.4432 0.3899 0.4045 -0.0650 -0.0682 -0.0242 199 ARG A O   
1407 C  CB  . ARG A 199 ? 0.4352 0.3917 0.4005 -0.0577 -0.0673 -0.0339 199 ARG A CB  
1408 C  CG  . ARG A 199 ? 0.4470 0.4049 0.4143 -0.0553 -0.0672 -0.0319 199 ARG A CG  
1409 C  CD  . ARG A 199 ? 0.4996 0.4572 0.4689 -0.0498 -0.0689 -0.0333 199 ARG A CD  
1410 N  NE  . ARG A 199 ? 0.4758 0.4340 0.4465 -0.0470 -0.0691 -0.0313 199 ARG A NE  
1411 C  CZ  . ARG A 199 ? 0.4876 0.4516 0.4595 -0.0456 -0.0683 -0.0342 199 ARG A CZ  
1412 N  NH1 . ARG A 199 ? 0.4648 0.4356 0.4377 -0.0465 -0.0671 -0.0394 199 ARG A NH1 
1413 N  NH2 . ARG A 199 ? 0.4945 0.4579 0.4669 -0.0432 -0.0686 -0.0319 199 ARG A NH2 
1414 N  N   . PHE A 200 ? 0.4144 0.3674 0.3752 -0.0665 -0.0647 -0.0254 200 PHE A N   
1415 C  CA  . PHE A 200 ? 0.3861 0.3348 0.3458 -0.0682 -0.0650 -0.0198 200 PHE A CA  
1416 C  C   . PHE A 200 ? 0.4231 0.3704 0.3790 -0.0727 -0.0643 -0.0196 200 PHE A C   
1417 O  O   . PHE A 200 ? 0.4618 0.4121 0.4154 -0.0751 -0.0623 -0.0232 200 PHE A O   
1418 C  CB  . PHE A 200 ? 0.3668 0.3167 0.3270 -0.0672 -0.0636 -0.0179 200 PHE A CB  
1419 C  CG  . PHE A 200 ? 0.3907 0.3407 0.3539 -0.0627 -0.0645 -0.0169 200 PHE A CG  
1420 C  CD1 . PHE A 200 ? 0.4243 0.3787 0.3890 -0.0601 -0.0643 -0.0211 200 PHE A CD1 
1421 C  CD2 . PHE A 200 ? 0.3814 0.3272 0.3460 -0.0609 -0.0656 -0.0117 200 PHE A CD2 
1422 C  CE1 . PHE A 200 ? 0.4117 0.3657 0.3785 -0.0557 -0.0653 -0.0202 200 PHE A CE1 
1423 C  CE2 . PHE A 200 ? 0.3929 0.3382 0.3594 -0.0568 -0.0663 -0.0109 200 PHE A CE2 
1424 C  CZ  . PHE A 200 ? 0.3909 0.3399 0.3582 -0.0542 -0.0662 -0.0150 200 PHE A CZ  
1425 N  N   . SER A 201 ? 0.4140 0.3568 0.3690 -0.0741 -0.0658 -0.0153 201 SER A N   
1426 C  CA  . SER A 201 ? 0.4179 0.3589 0.3688 -0.0781 -0.0653 -0.0144 201 SER A CA  
1427 C  C   . SER A 201 ? 0.4356 0.3729 0.3869 -0.0784 -0.0666 -0.0084 201 SER A C   
1428 O  O   . SER A 201 ? 0.4467 0.3826 0.4015 -0.0762 -0.0682 -0.0052 201 SER A O   
1429 C  CB  . SER A 201 ? 0.4423 0.3822 0.3906 -0.0802 -0.0661 -0.0173 201 SER A CB  
1430 O  OG  . SER A 201 ? 0.5410 0.4780 0.4916 -0.0788 -0.0689 -0.0153 201 SER A OG  
1431 N  N   . GLY A 202 ? 0.3990 0.3348 0.3463 -0.0812 -0.0657 -0.0069 202 GLY A N   
1432 C  CA  . GLY A 202 ? 0.4157 0.3486 0.3632 -0.0814 -0.0668 -0.0013 202 GLY A CA  
1433 C  C   . GLY A 202 ? 0.4144 0.3446 0.3574 -0.0848 -0.0678 -0.0007 202 GLY A C   
1434 O  O   . GLY A 202 ? 0.4233 0.3534 0.3616 -0.0873 -0.0663 -0.0042 202 GLY A O   
1435 N  N   . SER A 203 ? 0.3873 0.3153 0.3318 -0.0848 -0.0703 0.0035  203 SER A N   
1436 C  CA  . SER A 203 ? 0.4199 0.3452 0.3602 -0.0877 -0.0717 0.0046  203 SER A CA  
1437 C  C   . SER A 203 ? 0.4294 0.3534 0.3710 -0.0870 -0.0729 0.0105  203 SER A C   
1438 O  O   . SER A 203 ? 0.4168 0.3421 0.3634 -0.0843 -0.0729 0.0136  203 SER A O   
1439 C  CB  . SER A 203 ? 0.4481 0.3724 0.3887 -0.0889 -0.0744 0.0029  203 SER A CB  
1440 O  OG  . SER A 203 ? 0.4625 0.3869 0.4088 -0.0873 -0.0769 0.0061  203 SER A OG  
1441 N  N   . GLY A 204 ? 0.4386 0.3600 0.3759 -0.0892 -0.0742 0.0120  204 GLY A N   
1442 C  CA  . GLY A 204 ? 0.4546 0.3754 0.3939 -0.0885 -0.0762 0.0174  204 GLY A CA  
1443 C  C   . GLY A 204 ? 0.4317 0.3497 0.3649 -0.0892 -0.0749 0.0191  204 GLY A C   
1444 O  O   . GLY A 204 ? 0.4667 0.3831 0.3942 -0.0905 -0.0723 0.0162  204 GLY A O   
1445 N  N   . SER A 205 ? 0.4548 0.3722 0.3892 -0.0883 -0.0770 0.0239  205 SER A N   
1446 C  CA  . SER A 205 ? 0.4821 0.3964 0.4110 -0.0882 -0.0760 0.0263  205 SER A CA  
1447 C  C   . SER A 205 ? 0.4657 0.3814 0.3994 -0.0859 -0.0785 0.0320  205 SER A C   
1448 O  O   . SER A 205 ? 0.4740 0.3928 0.4141 -0.0857 -0.0812 0.0334  205 SER A O   
1449 C  CB  . SER A 205 ? 0.5179 0.4283 0.4385 -0.0915 -0.0769 0.0244  205 SER A CB  
1450 O  OG  . SER A 205 ? 0.5180 0.4290 0.4405 -0.0928 -0.0809 0.0253  205 SER A OG  
1451 N  N   . GLY A 206 ? 0.4979 0.4114 0.4284 -0.0843 -0.0773 0.0350  206 GLY A N   
1452 C  CA  . GLY A 206 ? 0.4974 0.4124 0.4318 -0.0821 -0.0797 0.0403  206 GLY A CA  
1453 C  C   . GLY A 206 ? 0.4700 0.3894 0.4133 -0.0788 -0.0789 0.0430  206 GLY A C   
1454 O  O   . GLY A 206 ? 0.4495 0.3682 0.3924 -0.0764 -0.0758 0.0438  206 GLY A O   
1455 N  N   . THR A 207 ? 0.4627 0.3863 0.4136 -0.0790 -0.0817 0.0446  207 THR A N   
1456 C  CA  . THR A 207 ? 0.4465 0.3742 0.4058 -0.0764 -0.0809 0.0471  207 THR A CA  
1457 C  C   . THR A 207 ? 0.4418 0.3710 0.4049 -0.0775 -0.0808 0.0439  207 THR A C   
1458 O  O   . THR A 207 ? 0.5001 0.4318 0.4692 -0.0755 -0.0799 0.0457  207 THR A O   
1459 C  CB  . THR A 207 ? 0.4859 0.4176 0.4519 -0.0753 -0.0838 0.0521  207 THR A CB  
1460 O  OG1 . THR A 207 ? 0.4633 0.3956 0.4298 -0.0787 -0.0878 0.0507  207 THR A OG1 
1461 C  CG2 . THR A 207 ? 0.4742 0.4051 0.4377 -0.0730 -0.0838 0.0557  207 THR A CG2 
1462 N  N   . ASP A 208 ? 0.4197 0.3473 0.3795 -0.0806 -0.0821 0.0397  208 ASP A N   
1463 C  CA  A ASP A 208 ? 0.4459 0.3746 0.4094 -0.0814 -0.0826 0.0371  208 ASP A CA  
1464 C  CA  B ASP A 208 ? 0.4244 0.3532 0.3879 -0.0813 -0.0826 0.0371  208 ASP A CA  
1465 C  C   . ASP A 208 ? 0.4277 0.3544 0.3864 -0.0819 -0.0801 0.0318  208 ASP A C   
1466 O  O   . ASP A 208 ? 0.4471 0.3714 0.3992 -0.0842 -0.0799 0.0288  208 ASP A O   
1467 C  CB  A ASP A 208 ? 0.4995 0.4281 0.4636 -0.0845 -0.0865 0.0361  208 ASP A CB  
1468 C  CB  B ASP A 208 ? 0.4313 0.3605 0.3967 -0.0841 -0.0866 0.0370  208 ASP A CB  
1469 C  CG  A ASP A 208 ? 0.5756 0.5060 0.5426 -0.0852 -0.0900 0.0403  208 ASP A CG  
1470 C  CG  B ASP A 208 ? 0.4378 0.3706 0.4108 -0.0835 -0.0890 0.0420  208 ASP A CG  
1471 O  OD1 A ASP A 208 ? 0.6186 0.5524 0.5920 -0.0831 -0.0899 0.0446  208 ASP A OD1 
1472 O  OD1 B ASP A 208 ? 0.4555 0.3901 0.4304 -0.0812 -0.0881 0.0459  208 ASP A OD1 
1473 O  OD2 A ASP A 208 ? 0.6490 0.5777 0.6121 -0.0879 -0.0928 0.0392  208 ASP A OD2 
1474 O  OD2 B ASP A 208 ? 0.4621 0.3957 0.4387 -0.0854 -0.0917 0.0418  208 ASP A OD2 
1475 N  N   . PHE A 209 ? 0.3946 0.3226 0.3566 -0.0800 -0.0783 0.0306  209 PHE A N   
1476 C  CA  . PHE A 209 ? 0.3699 0.2971 0.3286 -0.0799 -0.0759 0.0258  209 PHE A CA  
1477 C  C   . PHE A 209 ? 0.3972 0.3255 0.3600 -0.0791 -0.0765 0.0239  209 PHE A C   
1478 O  O   . PHE A 209 ? 0.3921 0.3215 0.3607 -0.0777 -0.0776 0.0272  209 PHE A O   
1479 C  CB  . PHE A 209 ? 0.3961 0.3232 0.3531 -0.0776 -0.0725 0.0263  209 PHE A CB  
1480 C  CG  . PHE A 209 ? 0.3904 0.3153 0.3424 -0.0785 -0.0720 0.0282  209 PHE A CG  
1481 C  CD1 . PHE A 209 ? 0.3752 0.2978 0.3201 -0.0809 -0.0708 0.0247  209 PHE A CD1 
1482 C  CD2 . PHE A 209 ? 0.4009 0.3260 0.3551 -0.0768 -0.0727 0.0334  209 PHE A CD2 
1483 C  CE1 . PHE A 209 ? 0.4092 0.3288 0.3486 -0.0817 -0.0703 0.0265  209 PHE A CE1 
1484 C  CE2 . PHE A 209 ? 0.4137 0.3363 0.3627 -0.0772 -0.0725 0.0351  209 PHE A CE2 
1485 C  CZ  . PHE A 209 ? 0.4035 0.3229 0.3448 -0.0797 -0.0713 0.0317  209 PHE A CZ  
1486 N  N   . THR A 210 ? 0.3971 0.3251 0.3572 -0.0797 -0.0756 0.0188  210 THR A N   
1487 C  CA  . THR A 210 ? 0.3894 0.3176 0.3523 -0.0787 -0.0763 0.0165  210 THR A CA  
1488 C  C   . THR A 210 ? 0.4087 0.3380 0.3698 -0.0772 -0.0738 0.0121  210 THR A C   
1489 O  O   . THR A 210 ? 0.3916 0.3210 0.3481 -0.0790 -0.0727 0.0085  210 THR A O   
1490 C  CB  . THR A 210 ? 0.3958 0.3224 0.3576 -0.0812 -0.0791 0.0145  210 THR A CB  
1491 O  OG1 . THR A 210 ? 0.3942 0.3203 0.3576 -0.0829 -0.0816 0.0186  210 THR A OG1 
1492 C  CG2 . THR A 210 ? 0.3906 0.3164 0.3555 -0.0800 -0.0802 0.0132  210 THR A CG2 
1493 N  N   . LEU A 211 ? 0.3792 0.3093 0.3436 -0.0743 -0.0732 0.0120  211 LEU A N   
1494 C  CA  . LEU A 211 ? 0.3662 0.2977 0.3296 -0.0726 -0.0716 0.0075  211 LEU A CA  
1495 C  C   . LEU A 211 ? 0.3880 0.3188 0.3524 -0.0722 -0.0732 0.0046  211 LEU A C   
1496 O  O   . LEU A 211 ? 0.3838 0.3127 0.3512 -0.0715 -0.0750 0.0070  211 LEU A O   
1497 C  CB  . LEU A 211 ? 0.3539 0.2862 0.3197 -0.0692 -0.0700 0.0097  211 LEU A CB  
1498 C  CG  . LEU A 211 ? 0.3589 0.2931 0.3244 -0.0669 -0.0687 0.0056  211 LEU A CG  
1499 C  CD1 . LEU A 211 ? 0.3661 0.3026 0.3278 -0.0685 -0.0667 0.0017  211 LEU A CD1 
1500 C  CD2 . LEU A 211 ? 0.3747 0.3087 0.3422 -0.0633 -0.0677 0.0080  211 LEU A CD2 
1501 N  N   . ASN A 212 ? 0.3756 0.3077 0.3376 -0.0724 -0.0725 -0.0006 212 ASN A N   
1502 C  CA  . ASN A 212 ? 0.4209 0.3521 0.3832 -0.0714 -0.0738 -0.0039 212 ASN A CA  
1503 C  C   . ASN A 212 ? 0.4256 0.3599 0.3884 -0.0684 -0.0722 -0.0079 212 ASN A C   
1504 O  O   . ASN A 212 ? 0.3960 0.3335 0.3572 -0.0690 -0.0702 -0.0102 212 ASN A O   
1505 C  CB  . ASN A 212 ? 0.3871 0.3173 0.3460 -0.0744 -0.0748 -0.0070 212 ASN A CB  
1506 C  CG  . ASN A 212 ? 0.4154 0.3416 0.3749 -0.0760 -0.0777 -0.0039 212 ASN A CG  
1507 O  OD1 . ASN A 212 ? 0.4093 0.3330 0.3700 -0.0748 -0.0793 -0.0046 212 ASN A OD1 
1508 N  ND2 . ASN A 212 ? 0.3841 0.3095 0.3426 -0.0789 -0.0785 -0.0008 212 ASN A ND2 
1509 N  N   . ILE A 213 ? 0.3920 0.3250 0.3567 -0.0654 -0.0733 -0.0089 213 ILE A N   
1510 C  CA  . ILE A 213 ? 0.3918 0.3277 0.3569 -0.0621 -0.0724 -0.0129 213 ILE A CA  
1511 C  C   . ILE A 213 ? 0.4244 0.3583 0.3890 -0.0607 -0.0740 -0.0162 213 ILE A C   
1512 O  O   . ILE A 213 ? 0.4045 0.3337 0.3698 -0.0598 -0.0758 -0.0138 213 ILE A O   
1513 C  CB  . ILE A 213 ? 0.3796 0.3153 0.3471 -0.0585 -0.0721 -0.0102 213 ILE A CB  
1514 C  CG1 . ILE A 213 ? 0.3992 0.3346 0.3673 -0.0597 -0.0710 -0.0053 213 ILE A CG1 
1515 C  CG2 . ILE A 213 ? 0.3933 0.3330 0.3612 -0.0553 -0.0712 -0.0145 213 ILE A CG2 
1516 C  CD1 . ILE A 213 ? 0.3942 0.3288 0.3641 -0.0562 -0.0706 -0.0024 213 ILE A CD1 
1517 N  N   . HIS A 214 ? 0.4228 0.3599 0.3859 -0.0605 -0.0731 -0.0216 214 HIS A N   
1518 C  CA  . HIS A 214 ? 0.4420 0.3769 0.4042 -0.0587 -0.0744 -0.0249 214 HIS A CA  
1519 C  C   . HIS A 214 ? 0.4758 0.4163 0.4376 -0.0574 -0.0728 -0.0309 214 HIS A C   
1520 O  O   . HIS A 214 ? 0.4612 0.4058 0.4219 -0.0603 -0.0709 -0.0327 214 HIS A O   
1521 C  CB  . HIS A 214 ? 0.4549 0.3853 0.4143 -0.0621 -0.0759 -0.0244 214 HIS A CB  
1522 C  CG  . HIS A 214 ? 0.5216 0.4494 0.4790 -0.0604 -0.0769 -0.0285 214 HIS A CG  
1523 N  ND1 . HIS A 214 ? 0.5272 0.4580 0.4824 -0.0608 -0.0756 -0.0338 214 HIS A ND1 
1524 C  CD2 . HIS A 214 ? 0.5038 0.4261 0.4609 -0.0580 -0.0790 -0.0282 214 HIS A CD2 
1525 C  CE1 . HIS A 214 ? 0.5693 0.4967 0.5230 -0.0583 -0.0769 -0.0365 214 HIS A CE1 
1526 N  NE2 . HIS A 214 ? 0.5358 0.4575 0.4902 -0.0567 -0.0790 -0.0332 214 HIS A NE2 
1527 N  N   . PRO A 215 ? 0.5155 0.4569 0.4782 -0.0530 -0.0733 -0.0342 215 PRO A N   
1528 C  CA  . PRO A 215 ? 0.4993 0.4357 0.4629 -0.0492 -0.0753 -0.0321 215 PRO A CA  
1529 C  C   . PRO A 215 ? 0.4875 0.4254 0.4536 -0.0467 -0.0750 -0.0292 215 PRO A C   
1530 O  O   . PRO A 215 ? 0.4930 0.4371 0.4605 -0.0456 -0.0736 -0.0314 215 PRO A O   
1531 C  CB  . PRO A 215 ? 0.5320 0.4694 0.4949 -0.0451 -0.0757 -0.0375 215 PRO A CB  
1532 C  CG  . PRO A 215 ? 0.5792 0.5226 0.5414 -0.0474 -0.0737 -0.0422 215 PRO A CG  
1533 C  CD  . PRO A 215 ? 0.5291 0.4767 0.4922 -0.0513 -0.0719 -0.0402 215 PRO A CD  
1534 N  N   . VAL A 216 ? 0.4677 0.3999 0.4341 -0.0462 -0.0763 -0.0243 216 VAL A N   
1535 C  CA  . VAL A 216 ? 0.4498 0.3823 0.4178 -0.0437 -0.0760 -0.0213 216 VAL A CA  
1536 C  C   . VAL A 216 ? 0.5001 0.4350 0.4686 -0.0384 -0.0763 -0.0247 216 VAL A C   
1537 O  O   . VAL A 216 ? 0.4928 0.4250 0.4602 -0.0355 -0.0776 -0.0272 216 VAL A O   
1538 C  CB  . VAL A 216 ? 0.4775 0.4035 0.4458 -0.0440 -0.0771 -0.0155 216 VAL A CB  
1539 C  CG1 . VAL A 216 ? 0.5432 0.4685 0.5124 -0.0403 -0.0768 -0.0130 216 VAL A CG1 
1540 C  CG2 . VAL A 216 ? 0.4292 0.3549 0.3981 -0.0488 -0.0766 -0.0116 216 VAL A CG2 
1541 N  N   . GLU A 217 ? 0.4500 0.3897 0.4198 -0.0370 -0.0752 -0.0250 217 GLU A N   
1542 C  CA  . GLU A 217 ? 0.4719 0.4139 0.4423 -0.0318 -0.0758 -0.0275 217 GLU A CA  
1543 C  C   . GLU A 217 ? 0.4651 0.4039 0.4353 -0.0297 -0.0759 -0.0230 217 GLU A C   
1544 O  O   . GLU A 217 ? 0.4517 0.3884 0.4219 -0.0324 -0.0750 -0.0186 217 GLU A O   
1545 C  CB  . GLU A 217 ? 0.4901 0.4411 0.4621 -0.0320 -0.0744 -0.0320 217 GLU A CB  
1546 C  CG  . GLU A 217 ? 0.5857 0.5406 0.5579 -0.0340 -0.0738 -0.0368 217 GLU A CG  
1547 C  CD  . GLU A 217 ? 0.6267 0.5911 0.6009 -0.0339 -0.0724 -0.0419 217 GLU A CD  
1548 O  OE1 . GLU A 217 ? 0.7335 0.7017 0.7090 -0.0322 -0.0723 -0.0421 217 GLU A OE1 
1549 O  OE2 . GLU A 217 ? 0.7329 0.7009 0.7072 -0.0359 -0.0714 -0.0456 217 GLU A OE2 
1550 N  N   . GLU A 218 ? 0.5099 0.4484 0.4797 -0.0245 -0.0770 -0.0242 218 GLU A N   
1551 C  CA  . GLU A 218 ? 0.4838 0.4187 0.4526 -0.0220 -0.0772 -0.0203 218 GLU A CA  
1552 C  C   . GLU A 218 ? 0.4738 0.4123 0.4433 -0.0242 -0.0754 -0.0184 218 GLU A C   
1553 O  O   . GLU A 218 ? 0.4749 0.4092 0.4435 -0.0245 -0.0748 -0.0136 218 GLU A O   
1554 C  CB  . GLU A 218 ? 0.5616 0.4974 0.5296 -0.0159 -0.0788 -0.0234 218 GLU A CB  
1555 C  CG  . GLU A 218 ? 0.6196 0.5488 0.5852 -0.0123 -0.0795 -0.0194 218 GLU A CG  
1556 C  CD  . GLU A 218 ? 0.7083 0.6367 0.6724 -0.0063 -0.0817 -0.0228 218 GLU A CD  
1557 O  OE1 . GLU A 218 ? 0.7723 0.6938 0.7344 -0.0045 -0.0829 -0.0220 218 GLU A OE1 
1558 O  OE2 . GLU A 218 ? 0.7205 0.6553 0.6856 -0.0035 -0.0822 -0.0263 218 GLU A OE2 
1559 N  N   . GLU A 219 ? 0.4621 0.4081 0.4329 -0.0258 -0.0745 -0.0223 219 GLU A N   
1560 C  CA  A GLU A 219 ? 0.4386 0.3878 0.4093 -0.0283 -0.0728 -0.0213 219 GLU A CA  
1561 C  CA  B GLU A 219 ? 0.4355 0.3845 0.4062 -0.0282 -0.0728 -0.0210 219 GLU A CA  
1562 C  C   . GLU A 219 ? 0.4354 0.3811 0.4056 -0.0327 -0.0713 -0.0167 219 GLU A C   
1563 O  O   . GLU A 219 ? 0.4645 0.4106 0.4340 -0.0344 -0.0699 -0.0144 219 GLU A O   
1564 C  CB  A GLU A 219 ? 0.5259 0.4837 0.4980 -0.0292 -0.0722 -0.0268 219 GLU A CB  
1565 C  CB  B GLU A 219 ? 0.5157 0.4730 0.4877 -0.0299 -0.0719 -0.0262 219 GLU A CB  
1566 C  CG  A GLU A 219 ? 0.5636 0.5257 0.5367 -0.0337 -0.0709 -0.0298 219 GLU A CG  
1567 C  CG  B GLU A 219 ? 0.5638 0.5259 0.5362 -0.0264 -0.0727 -0.0293 219 GLU A CG  
1568 C  CD  A GLU A 219 ? 0.5937 0.5648 0.5686 -0.0346 -0.0701 -0.0357 219 GLU A CD  
1569 C  CD  B GLU A 219 ? 0.5521 0.5126 0.5227 -0.0254 -0.0723 -0.0265 219 GLU A CD  
1570 O  OE1 A GLU A 219 ? 0.6508 0.6255 0.6273 -0.0305 -0.0715 -0.0393 219 GLU A OE1 
1571 O  OE1 B GLU A 219 ? 0.5253 0.4871 0.4950 -0.0289 -0.0705 -0.0255 219 GLU A OE1 
1572 O  OE2 A GLU A 219 ? 0.5089 0.4837 0.4837 -0.0393 -0.0682 -0.0371 219 GLU A OE2 
1573 O  OE2 B GLU A 219 ? 0.6400 0.5976 0.6095 -0.0207 -0.0739 -0.0255 219 GLU A OE2 
1574 N  N   . ASP A 220 ? 0.4227 0.3651 0.3933 -0.0347 -0.0718 -0.0153 220 ASP A N   
1575 C  CA  . ASP A 220 ? 0.3804 0.3208 0.3509 -0.0391 -0.0707 -0.0115 220 ASP A CA  
1576 C  C   . ASP A 220 ? 0.3659 0.3006 0.3364 -0.0383 -0.0707 -0.0055 220 ASP A C   
1577 O  O   . ASP A 220 ? 0.3967 0.3299 0.3676 -0.0414 -0.0699 -0.0017 220 ASP A O   
1578 C  CB  . ASP A 220 ? 0.3779 0.3178 0.3486 -0.0422 -0.0713 -0.0128 220 ASP A CB  
1579 C  CG  . ASP A 220 ? 0.4555 0.4012 0.4261 -0.0434 -0.0708 -0.0186 220 ASP A CG  
1580 O  OD1 . ASP A 220 ? 0.4638 0.4145 0.4344 -0.0440 -0.0694 -0.0207 220 ASP A OD1 
1581 O  OD2 . ASP A 220 ? 0.4814 0.4267 0.4519 -0.0435 -0.0718 -0.0213 220 ASP A OD2 
1582 N  N   . ALA A 221 ? 0.4024 0.3339 0.3724 -0.0342 -0.0716 -0.0045 221 ALA A N   
1583 C  CA  . ALA A 221 ? 0.4180 0.3443 0.3878 -0.0334 -0.0711 0.0011  221 ALA A CA  
1584 C  C   . ALA A 221 ? 0.4206 0.3484 0.3899 -0.0339 -0.0691 0.0037  221 ALA A C   
1585 O  O   . ALA A 221 ? 0.4201 0.3504 0.3879 -0.0319 -0.0687 0.0015  221 ALA A O   
1586 C  CB  . ALA A 221 ? 0.4442 0.3665 0.4126 -0.0287 -0.0723 0.0013  221 ALA A CB  
1587 N  N   . ALA A 222 ? 0.3632 0.2896 0.3335 -0.0366 -0.0680 0.0081  222 ALA A N   
1588 C  CA  . ALA A 222 ? 0.3701 0.2977 0.3394 -0.0373 -0.0659 0.0102  222 ALA A CA  
1589 C  C   . ALA A 222 ? 0.4013 0.3267 0.3723 -0.0395 -0.0651 0.0155  222 ALA A C   
1590 O  O   . ALA A 222 ? 0.4276 0.3514 0.4007 -0.0410 -0.0663 0.0169  222 ALA A O   
1591 C  CB  . ALA A 222 ? 0.3824 0.3147 0.3508 -0.0399 -0.0654 0.0061  222 ALA A CB  
1592 N  N   . THR A 223 ? 0.3735 0.2990 0.3436 -0.0398 -0.0631 0.0183  223 THR A N   
1593 C  CA  . THR A 223 ? 0.3840 0.3090 0.3562 -0.0421 -0.0624 0.0228  223 THR A CA  
1594 C  C   . THR A 223 ? 0.3374 0.2650 0.3083 -0.0454 -0.0620 0.0211  223 THR A C   
1595 O  O   . THR A 223 ? 0.3579 0.2869 0.3259 -0.0452 -0.0610 0.0185  223 THR A O   
1596 C  CB  . THR A 223 ? 0.4033 0.3261 0.3750 -0.0397 -0.0603 0.0274  223 THR A CB  
1597 O  OG1 . THR A 223 ? 0.4458 0.3656 0.4183 -0.0372 -0.0607 0.0291  223 THR A OG1 
1598 C  CG2 . THR A 223 ? 0.3632 0.2861 0.3375 -0.0416 -0.0594 0.0322  223 THR A CG2 
1599 N  N   . TYR A 224 ? 0.3351 0.2632 0.3081 -0.0484 -0.0629 0.0225  224 TYR A N   
1600 C  CA  . TYR A 224 ? 0.3361 0.2659 0.3074 -0.0517 -0.0629 0.0210  224 TYR A CA  
1601 C  C   . TYR A 224 ? 0.3306 0.2596 0.3027 -0.0523 -0.0618 0.0261  224 TYR A C   
1602 O  O   . TYR A 224 ? 0.3523 0.2806 0.3279 -0.0520 -0.0623 0.0300  224 TYR A O   
1603 C  CB  . TYR A 224 ? 0.3239 0.2545 0.2962 -0.0544 -0.0650 0.0184  224 TYR A CB  
1604 C  CG  . TYR A 224 ? 0.3124 0.2443 0.2836 -0.0532 -0.0656 0.0131  224 TYR A CG  
1605 C  CD1 . TYR A 224 ? 0.3045 0.2391 0.2731 -0.0546 -0.0650 0.0085  224 TYR A CD1 
1606 C  CD2 . TYR A 224 ? 0.3465 0.2768 0.3192 -0.0509 -0.0669 0.0125  224 TYR A CD2 
1607 C  CE1 . TYR A 224 ? 0.3419 0.2787 0.3101 -0.0532 -0.0654 0.0036  224 TYR A CE1 
1608 C  CE2 . TYR A 224 ? 0.3487 0.2804 0.3204 -0.0493 -0.0676 0.0076  224 TYR A CE2 
1609 C  CZ  . TYR A 224 ? 0.3587 0.2942 0.3287 -0.0505 -0.0669 0.0030  224 TYR A CZ  
1610 O  OH  . TYR A 224 ? 0.3568 0.2946 0.3265 -0.0486 -0.0675 -0.0018 224 TYR A OH  
1611 N  N   . TYR A 225 ? 0.3237 0.2528 0.2924 -0.0530 -0.0602 0.0259  225 TYR A N   
1612 C  CA  . TYR A 225 ? 0.3312 0.2595 0.3002 -0.0534 -0.0593 0.0304  225 TYR A CA  
1613 C  C   . TYR A 225 ? 0.3481 0.2767 0.3142 -0.0566 -0.0596 0.0290  225 TYR A C   
1614 O  O   . TYR A 225 ? 0.3809 0.3097 0.3431 -0.0580 -0.0590 0.0249  225 TYR A O   
1615 C  CB  . TYR A 225 ? 0.3283 0.2548 0.2945 -0.0507 -0.0567 0.0323  225 TYR A CB  
1616 C  CG  . TYR A 225 ? 0.3424 0.2678 0.3102 -0.0471 -0.0558 0.0343  225 TYR A CG  
1617 C  CD1 . TYR A 225 ? 0.3342 0.2592 0.3058 -0.0455 -0.0553 0.0394  225 TYR A CD1 
1618 C  CD2 . TYR A 225 ? 0.3555 0.2804 0.3210 -0.0452 -0.0555 0.0310  225 TYR A CD2 
1619 C  CE1 . TYR A 225 ? 0.3559 0.2794 0.3283 -0.0423 -0.0541 0.0414  225 TYR A CE1 
1620 C  CE2 . TYR A 225 ? 0.3798 0.3030 0.3458 -0.0418 -0.0546 0.0329  225 TYR A CE2 
1621 C  CZ  . TYR A 225 ? 0.3802 0.3024 0.3494 -0.0404 -0.0539 0.0381  225 TYR A CZ  
1622 O  OH  . TYR A 225 ? 0.4094 0.3294 0.3783 -0.0370 -0.0527 0.0400  225 TYR A OH  
1623 N  N   . CYS A 226 ? 0.3573 0.2859 0.3250 -0.0580 -0.0605 0.0325  226 CYS A N   
1624 C  CA  . CYS A 226 ? 0.3673 0.2953 0.3313 -0.0606 -0.0606 0.0319  226 CYS A CA  
1625 C  C   . CYS A 226 ? 0.3690 0.2949 0.3304 -0.0587 -0.0585 0.0353  226 CYS A C   
1626 O  O   . CYS A 226 ? 0.3579 0.2836 0.3217 -0.0556 -0.0573 0.0387  226 CYS A O   
1627 C  CB  . CYS A 226 ? 0.3699 0.2988 0.3363 -0.0630 -0.0632 0.0334  226 CYS A CB  
1628 S  SG  . CYS A 226 ? 0.4251 0.3556 0.3985 -0.0612 -0.0642 0.0395  226 CYS A SG  
1629 N  N   . GLN A 227 ? 0.3435 0.2674 0.2995 -0.0606 -0.0578 0.0342  227 GLN A N   
1630 C  CA  . GLN A 227 ? 0.3701 0.2910 0.3223 -0.0589 -0.0557 0.0369  227 GLN A CA  
1631 C  C   . GLN A 227 ? 0.3769 0.2958 0.3249 -0.0613 -0.0563 0.0373  227 GLN A C   
1632 O  O   . GLN A 227 ? 0.3855 0.3043 0.3306 -0.0646 -0.0570 0.0335  227 GLN A O   
1633 C  CB  . GLN A 227 ? 0.3768 0.2957 0.3241 -0.0585 -0.0534 0.0336  227 GLN A CB  
1634 C  CG  . GLN A 227 ? 0.3739 0.2885 0.3160 -0.0569 -0.0511 0.0360  227 GLN A CG  
1635 C  CD  . GLN A 227 ? 0.4947 0.4058 0.4293 -0.0598 -0.0501 0.0333  227 GLN A CD  
1636 O  OE1 . GLN A 227 ? 0.5213 0.4284 0.4506 -0.0589 -0.0480 0.0335  227 GLN A OE1 
1637 N  NE2 . GLN A 227 ? 0.4608 0.3727 0.3942 -0.0634 -0.0515 0.0311  227 GLN A NE2 
1638 N  N   . GLN A 228 ? 0.3882 0.3052 0.3352 -0.0595 -0.0558 0.0416  228 GLN A N   
1639 C  CA  . GLN A 228 ? 0.3743 0.2880 0.3155 -0.0614 -0.0560 0.0419  228 GLN A CA  
1640 C  C   . GLN A 228 ? 0.3964 0.3051 0.3309 -0.0598 -0.0531 0.0426  228 GLN A C   
1641 O  O   . GLN A 228 ? 0.3724 0.2804 0.3083 -0.0562 -0.0516 0.0453  228 GLN A O   
1642 C  CB  . GLN A 228 ? 0.3744 0.2895 0.3188 -0.0610 -0.0583 0.0459  228 GLN A CB  
1643 C  CG  . GLN A 228 ? 0.3894 0.3054 0.3376 -0.0568 -0.0576 0.0513  228 GLN A CG  
1644 C  CD  . GLN A 228 ? 0.3901 0.3010 0.3317 -0.0549 -0.0557 0.0534  228 GLN A CD  
1645 O  OE1 . GLN A 228 ? 0.4259 0.3329 0.3606 -0.0571 -0.0559 0.0520  228 GLN A OE1 
1646 N  NE2 . GLN A 228 ? 0.4009 0.3113 0.3437 -0.0509 -0.0536 0.0566  228 GLN A NE2 
1647 N  N   . ASN A 229 ? 0.3860 0.2906 0.3130 -0.0626 -0.0526 0.0404  229 ASN A N   
1648 C  CA  . ASN A 229 ? 0.4111 0.3096 0.3305 -0.0616 -0.0500 0.0411  229 ASN A CA  
1649 C  C   . ASN A 229 ? 0.4523 0.3462 0.3653 -0.0631 -0.0506 0.0424  229 ASN A C   
1650 O  O   . ASN A 229 ? 0.4539 0.3418 0.3584 -0.0644 -0.0486 0.0412  229 ASN A O   
1651 C  CB  . ASN A 229 ? 0.4264 0.3232 0.3416 -0.0632 -0.0478 0.0367  229 ASN A CB  
1652 C  CG  . ASN A 229 ? 0.5044 0.4018 0.4165 -0.0681 -0.0481 0.0316  229 ASN A CG  
1653 O  OD1 . ASN A 229 ? 0.4976 0.3998 0.4146 -0.0697 -0.0500 0.0297  229 ASN A OD1 
1654 N  ND2 . ASN A 229 ? 0.4922 0.3845 0.3960 -0.0708 -0.0463 0.0295  229 ASN A ND2 
1655 N  N   . ASN A 230 ? 0.4270 0.3234 0.3435 -0.0632 -0.0533 0.0448  230 ASN A N   
1656 C  CA  . ASN A 230 ? 0.4767 0.3689 0.3876 -0.0637 -0.0543 0.0468  230 ASN A CA  
1657 C  C   . ASN A 230 ? 0.5131 0.4018 0.4220 -0.0592 -0.0532 0.0516  230 ASN A C   
1658 O  O   . ASN A 230 ? 0.5393 0.4216 0.4401 -0.0593 -0.0526 0.0526  230 ASN A O   
1659 C  CB  . ASN A 230 ? 0.4683 0.3648 0.3840 -0.0651 -0.0579 0.0478  230 ASN A CB  
1660 C  CG  . ASN A 230 ? 0.5057 0.3974 0.4142 -0.0667 -0.0592 0.0486  230 ASN A CG  
1661 O  OD1 . ASN A 230 ? 0.4982 0.3843 0.3978 -0.0694 -0.0576 0.0460  230 ASN A OD1 
1662 N  ND2 . ASN A 230 ? 0.5062 0.4002 0.4183 -0.0650 -0.0621 0.0523  230 ASN A ND2 
1663 N  N   . GLU A 231 ? 0.4827 0.3755 0.3991 -0.0552 -0.0530 0.0548  231 GLU A N   
1664 C  CA  . GLU A 231 ? 0.5400 0.4307 0.4559 -0.0504 -0.0520 0.0596  231 GLU A CA  
1665 C  C   . GLU A 231 ? 0.5374 0.4285 0.4556 -0.0472 -0.0492 0.0602  231 GLU A C   
1666 O  O   . GLU A 231 ? 0.4970 0.3924 0.4205 -0.0481 -0.0492 0.0582  231 GLU A O   
1667 C  CB  . GLU A 231 ? 0.5381 0.4351 0.4626 -0.0484 -0.0549 0.0637  231 GLU A CB  
1668 C  CG  . GLU A 231 ? 0.7064 0.6019 0.6274 -0.0503 -0.0578 0.0643  231 GLU A CG  
1669 C  CD  . GLU A 231 ? 0.7401 0.6425 0.6699 -0.0489 -0.0612 0.0679  231 GLU A CD  
1670 O  OE1 . GLU A 231 ? 0.6786 0.5849 0.6150 -0.0449 -0.0604 0.0716  231 GLU A OE1 
1671 O  OE2 . GLU A 231 ? 0.8353 0.7392 0.7653 -0.0519 -0.0644 0.0670  231 GLU A OE2 
1672 N  N   . ASP A 232 ? 0.5005 0.3866 0.4142 -0.0433 -0.0469 0.0629  232 ASP A N   
1673 C  CA  . ASP A 232 ? 0.4999 0.3862 0.4156 -0.0397 -0.0442 0.0641  232 ASP A CA  
1674 C  C   . ASP A 232 ? 0.4909 0.3836 0.4161 -0.0357 -0.0448 0.0687  232 ASP A C   
1675 O  O   . ASP A 232 ? 0.5093 0.4037 0.4367 -0.0343 -0.0465 0.0719  232 ASP A O   
1676 C  CB  . ASP A 232 ? 0.5578 0.4353 0.4639 -0.0371 -0.0412 0.0648  232 ASP A CB  
1677 C  CG  . ASP A 232 ? 0.6542 0.5254 0.5510 -0.0414 -0.0401 0.0600  232 ASP A CG  
1678 O  OD1 . ASP A 232 ? 0.6577 0.5312 0.5562 -0.0437 -0.0397 0.0563  232 ASP A OD1 
1679 O  OD2 . ASP A 232 ? 0.7680 0.6327 0.6565 -0.0427 -0.0400 0.0598  232 ASP A OD2 
1680 N  N   . PRO A 233 ? 0.4340 0.3304 0.3651 -0.0338 -0.0435 0.0693  233 PRO A N   
1681 C  CA  . PRO A 233 ? 0.4141 0.3089 0.3429 -0.0355 -0.0420 0.0653  233 PRO A CA  
1682 C  C   . PRO A 233 ? 0.4109 0.3100 0.3433 -0.0402 -0.0446 0.0615  233 PRO A C   
1683 O  O   . PRO A 233 ? 0.4216 0.3264 0.3613 -0.0411 -0.0471 0.0628  233 PRO A O   
1684 C  CB  . PRO A 233 ? 0.4299 0.3285 0.3654 -0.0314 -0.0404 0.0683  233 PRO A CB  
1685 C  CG  . PRO A 233 ? 0.4364 0.3421 0.3813 -0.0307 -0.0425 0.0721  233 PRO A CG  
1686 C  CD  . PRO A 233 ? 0.4344 0.3370 0.3747 -0.0301 -0.0433 0.0738  233 PRO A CD  
1687 N  N   . ARG A 234 ? 0.4371 0.3341 0.3654 -0.0428 -0.0438 0.0568  234 ARG A N   
1688 C  CA  A ARG A 234 ? 0.3979 0.2995 0.3305 -0.0462 -0.0458 0.0532  234 ARG A CA  
1689 C  CA  B ARG A 234 ? 0.4060 0.3075 0.3386 -0.0462 -0.0458 0.0532  234 ARG A CA  
1690 C  C   . ARG A 234 ? 0.4071 0.3143 0.3489 -0.0441 -0.0465 0.0555  234 ARG A C   
1691 O  O   . ARG A 234 ? 0.4035 0.3106 0.3470 -0.0404 -0.0445 0.0583  234 ARG A O   
1692 C  CB  A ARG A 234 ? 0.4059 0.3050 0.3337 -0.0480 -0.0444 0.0484  234 ARG A CB  
1693 C  CB  B ARG A 234 ? 0.4255 0.3251 0.3542 -0.0473 -0.0443 0.0488  234 ARG A CB  
1694 C  CG  A ARG A 234 ? 0.4457 0.3388 0.3639 -0.0505 -0.0432 0.0456  234 ARG A CG  
1695 C  CG  B ARG A 234 ? 0.5027 0.3976 0.4229 -0.0508 -0.0436 0.0449  234 ARG A CG  
1696 C  CD  A ARG A 234 ? 0.4361 0.3275 0.3505 -0.0515 -0.0416 0.0414  234 ARG A CD  
1697 C  CD  B ARG A 234 ? 0.4893 0.3834 0.4070 -0.0514 -0.0423 0.0410  234 ARG A CD  
1698 N  NE  A ARG A 234 ? 0.5107 0.3960 0.4158 -0.0542 -0.0402 0.0390  234 ARG A NE  
1699 N  NE  B ARG A 234 ? 0.4741 0.3677 0.3876 -0.0562 -0.0426 0.0360  234 ARG A NE  
1700 C  CZ  A ARG A 234 ? 0.5060 0.3918 0.4084 -0.0588 -0.0406 0.0345  234 ARG A CZ  
1701 C  CZ  B ARG A 234 ? 0.5102 0.3983 0.4158 -0.0584 -0.0413 0.0350  234 ARG A CZ  
1702 N  NH1 A ARG A 234 ? 0.5271 0.4193 0.4355 -0.0608 -0.0425 0.0319  234 ARG A NH1 
1703 N  NH1 B ARG A 234 ? 0.5669 0.4491 0.4676 -0.0559 -0.0400 0.0387  234 ARG A NH1 
1704 N  NH2 A ARG A 234 ? 0.4828 0.3623 0.3762 -0.0614 -0.0390 0.0329  234 ARG A NH2 
1705 N  NH2 B ARG A 234 ? 0.5618 0.4501 0.4640 -0.0630 -0.0414 0.0304  234 ARG A NH2 
1706 N  N   . THR A 235 ? 0.3914 0.3034 0.3388 -0.0467 -0.0492 0.0544  235 THR A N   
1707 C  CA  . THR A 235 ? 0.4052 0.3220 0.3609 -0.0454 -0.0499 0.0563  235 THR A CA  
1708 C  C   . THR A 235 ? 0.3906 0.3098 0.3486 -0.0484 -0.0517 0.0522  235 THR A C   
1709 O  O   . THR A 235 ? 0.3898 0.3084 0.3445 -0.0517 -0.0530 0.0484  235 THR A O   
1710 C  CB  . THR A 235 ? 0.4153 0.3359 0.3770 -0.0447 -0.0516 0.0609  235 THR A CB  
1711 O  OG1 . THR A 235 ? 0.4025 0.3237 0.3633 -0.0481 -0.0544 0.0596  235 THR A OG1 
1712 C  CG2 . THR A 235 ? 0.4049 0.3239 0.3656 -0.0408 -0.0496 0.0653  235 THR A CG2 
1713 N  N   . PHE A 236 ? 0.3609 0.2828 0.3245 -0.0470 -0.0518 0.0531  236 PHE A N   
1714 C  CA  . PHE A 236 ? 0.3298 0.2534 0.2954 -0.0489 -0.0533 0.0494  236 PHE A CA  
1715 C  C   . PHE A 236 ? 0.3523 0.2796 0.3254 -0.0492 -0.0552 0.0520  236 PHE A C   
1716 O  O   . PHE A 236 ? 0.3804 0.3092 0.3577 -0.0470 -0.0543 0.0566  236 PHE A O   
1717 C  CB  . PHE A 236 ? 0.3446 0.2666 0.3083 -0.0467 -0.0515 0.0476  236 PHE A CB  
1718 C  CG  . PHE A 236 ? 0.3612 0.2797 0.3175 -0.0468 -0.0498 0.0444  236 PHE A CG  
1719 C  CD1 . PHE A 236 ? 0.3596 0.2746 0.3117 -0.0444 -0.0473 0.0467  236 PHE A CD1 
1720 C  CD2 . PHE A 236 ? 0.3671 0.2859 0.3207 -0.0492 -0.0506 0.0391  236 PHE A CD2 
1721 C  CE1 . PHE A 236 ? 0.3767 0.2881 0.3217 -0.0449 -0.0459 0.0437  236 PHE A CE1 
1722 C  CE2 . PHE A 236 ? 0.3702 0.2863 0.3175 -0.0496 -0.0490 0.0361  236 PHE A CE2 
1723 C  CZ  . PHE A 236 ? 0.3638 0.2760 0.3067 -0.0477 -0.0468 0.0384  236 PHE A CZ  
1724 N  N   . GLY A 237 ? 0.3281 0.2566 0.3028 -0.0517 -0.0574 0.0488  237 GLY A N   
1725 C  CA  . GLY A 237 ? 0.3379 0.2689 0.3191 -0.0523 -0.0591 0.0506  237 GLY A CA  
1726 C  C   . GLY A 237 ? 0.3619 0.2922 0.3448 -0.0494 -0.0574 0.0515  237 GLY A C   
1727 O  O   . GLY A 237 ? 0.3781 0.3062 0.3573 -0.0470 -0.0551 0.0507  237 GLY A O   
1728 N  N   . GLY A 238 ? 0.3850 0.3169 0.3735 -0.0497 -0.0584 0.0536  238 GLY A N   
1729 C  CA  . GLY A 238 ? 0.3631 0.2939 0.3531 -0.0468 -0.0565 0.0555  238 GLY A CA  
1730 C  C   . GLY A 238 ? 0.3809 0.3094 0.3683 -0.0465 -0.0570 0.0513  238 GLY A C   
1731 O  O   . GLY A 238 ? 0.4158 0.3424 0.4028 -0.0439 -0.0555 0.0521  238 GLY A O   
1732 N  N   . GLY A 239 ? 0.3688 0.2974 0.3541 -0.0489 -0.0592 0.0468  239 GLY A N   
1733 C  CA  . GLY A 239 ? 0.3693 0.2963 0.3521 -0.0483 -0.0598 0.0424  239 GLY A CA  
1734 C  C   . GLY A 239 ? 0.4034 0.3301 0.3893 -0.0500 -0.0623 0.0415  239 GLY A C   
1735 O  O   . GLY A 239 ? 0.4025 0.3294 0.3926 -0.0507 -0.0628 0.0452  239 GLY A O   
1736 N  N   . THR A 240 ? 0.3433 0.2694 0.3267 -0.0506 -0.0637 0.0366  240 THR A N   
1737 C  CA  . THR A 240 ? 0.3460 0.2707 0.3310 -0.0516 -0.0659 0.0351  240 THR A CA  
1738 C  C   . THR A 240 ? 0.3384 0.2613 0.3205 -0.0487 -0.0656 0.0316  240 THR A C   
1739 O  O   . THR A 240 ? 0.3659 0.2901 0.3451 -0.0484 -0.0656 0.0274  240 THR A O   
1740 C  CB  . THR A 240 ? 0.3432 0.2691 0.3276 -0.0551 -0.0681 0.0320  240 THR A CB  
1741 O  OG1 . THR A 240 ? 0.3823 0.3098 0.3693 -0.0575 -0.0686 0.0355  240 THR A OG1 
1742 C  CG2 . THR A 240 ? 0.3735 0.2972 0.3586 -0.0558 -0.0703 0.0300  240 THR A CG2 
1743 N  N   . LYS A 241 ? 0.3546 0.2745 0.3377 -0.0468 -0.0658 0.0332  241 LYS A N   
1744 C  CA  . LYS A 241 ? 0.3655 0.2834 0.3458 -0.0436 -0.0659 0.0301  241 LYS A CA  
1745 C  C   . LYS A 241 ? 0.4014 0.3178 0.3813 -0.0445 -0.0684 0.0265  241 LYS A C   
1746 O  O   . LYS A 241 ? 0.4161 0.3296 0.3978 -0.0458 -0.0696 0.0284  241 LYS A O   
1747 C  CB  . LYS A 241 ? 0.4115 0.3260 0.3918 -0.0406 -0.0644 0.0340  241 LYS A CB  
1748 C  CG  . LYS A 241 ? 0.4958 0.4077 0.4727 -0.0370 -0.0649 0.0310  241 LYS A CG  
1749 C  CD  . LYS A 241 ? 0.5406 0.4489 0.5163 -0.0337 -0.0631 0.0346  241 LYS A CD  
1750 C  CE  . LYS A 241 ? 0.6859 0.5908 0.6579 -0.0300 -0.0641 0.0317  241 LYS A CE  
1751 N  NZ  . LYS A 241 ? 0.6303 0.5316 0.5999 -0.0267 -0.0622 0.0350  241 LYS A NZ  
1752 N  N   . LEU A 242 ? 0.3893 0.3074 0.3668 -0.0437 -0.0690 0.0213  242 LEU A N   
1753 C  CA  . LEU A 242 ? 0.4032 0.3200 0.3798 -0.0439 -0.0712 0.0173  242 LEU A CA  
1754 C  C   . LEU A 242 ? 0.4193 0.3337 0.3937 -0.0395 -0.0715 0.0153  242 LEU A C   
1755 O  O   . LEU A 242 ? 0.4211 0.3378 0.3939 -0.0370 -0.0706 0.0131  242 LEU A O   
1756 C  CB  . LEU A 242 ? 0.3839 0.3049 0.3594 -0.0459 -0.0715 0.0127  242 LEU A CB  
1757 C  CG  . LEU A 242 ? 0.4047 0.3253 0.3789 -0.0456 -0.0732 0.0077  242 LEU A CG  
1758 C  CD1 . LEU A 242 ? 0.3994 0.3159 0.3744 -0.0477 -0.0751 0.0090  242 LEU A CD1 
1759 C  CD2 . LEU A 242 ? 0.4147 0.3401 0.3878 -0.0473 -0.0729 0.0029  242 LEU A CD2 
1760 N  N   . GLU A 243 ? 0.4047 0.3141 0.3787 -0.0387 -0.0729 0.0157  243 GLU A N   
1761 C  CA  . GLU A 243 ? 0.4389 0.3455 0.4103 -0.0343 -0.0737 0.0133  243 GLU A CA  
1762 C  C   . GLU A 243 ? 0.4536 0.3588 0.4237 -0.0342 -0.0758 0.0088  243 GLU A C   
1763 O  O   . GLU A 243 ? 0.4460 0.3508 0.4172 -0.0377 -0.0767 0.0087  243 GLU A O   
1764 C  CB  . GLU A 243 ? 0.4900 0.3905 0.4608 -0.0326 -0.0733 0.0178  243 GLU A CB  
1765 C  CG  . GLU A 243 ? 0.5723 0.4737 0.5430 -0.0311 -0.0710 0.0213  243 GLU A CG  
1766 C  CD  . GLU A 243 ? 0.6367 0.5323 0.6070 -0.0300 -0.0701 0.0262  243 GLU A CD  
1767 O  OE1 . GLU A 243 ? 0.6957 0.5878 0.6626 -0.0258 -0.0701 0.0258  243 GLU A OE1 
1768 O  OE2 . GLU A 243 ? 0.6195 0.5142 0.5927 -0.0331 -0.0694 0.0303  243 GLU A OE2 
1769 N  N   . ILE A 244 ? 0.4526 0.3569 0.4203 -0.0299 -0.0767 0.0053  244 ILE A N   
1770 C  CA  . ILE A 244 ? 0.4779 0.3801 0.4441 -0.0289 -0.0786 0.0012  244 ILE A CA  
1771 C  C   . ILE A 244 ? 0.4884 0.3820 0.4527 -0.0283 -0.0797 0.0040  244 ILE A C   
1772 O  O   . ILE A 244 ? 0.5274 0.4168 0.4901 -0.0254 -0.0793 0.0067  244 ILE A O   
1773 C  CB  . ILE A 244 ? 0.5322 0.4376 0.4969 -0.0243 -0.0791 -0.0037 244 ILE A CB  
1774 C  CG1 . ILE A 244 ? 0.5460 0.4603 0.5126 -0.0257 -0.0779 -0.0066 244 ILE A CG1 
1775 C  CG2 . ILE A 244 ? 0.5533 0.4559 0.5160 -0.0224 -0.0810 -0.0077 244 ILE A CG2 
1776 C  CD1 . ILE A 244 ? 0.5586 0.4759 0.5268 -0.0309 -0.0774 -0.0073 244 ILE A CD1 
1777 N  N   . LYS A 245 ? 0.4845 0.3748 0.4486 -0.0312 -0.0810 0.0034  245 LYS A N   
1778 C  CA  . LYS A 245 ? 0.4475 0.3289 0.4093 -0.0309 -0.0822 0.0054  245 LYS A CA  
1779 C  C   . LYS A 245 ? 0.5511 0.4291 0.5089 -0.0260 -0.0836 0.0009  245 LYS A C   
1780 O  O   . LYS A 245 ? 0.5963 0.4761 0.5535 -0.0260 -0.0846 -0.0035 245 LYS A O   
1781 C  CB  . LYS A 245 ? 0.4598 0.3388 0.4227 -0.0363 -0.0832 0.0066  245 LYS A CB  
1782 C  CG  . LYS A 245 ? 0.5063 0.3760 0.4671 -0.0374 -0.0844 0.0093  245 LYS A CG  
1783 C  CD  . LYS A 245 ? 0.5284 0.3978 0.4917 -0.0436 -0.0852 0.0114  245 LYS A CD  
1784 C  CE  . LYS A 245 ? 0.5569 0.4173 0.5184 -0.0459 -0.0865 0.0140  245 LYS A CE  
1785 N  NZ  . LYS A 245 ? 0.6110 0.4648 0.5676 -0.0450 -0.0886 0.0099  245 LYS A NZ  
1786 N  N   . LEU A 246 ? 0.5872 0.4602 0.5422 -0.0216 -0.0837 0.0023  246 LEU A N   
1787 C  CA  . LEU A 246 ? 0.7208 0.5899 0.6716 -0.0159 -0.0851 -0.0012 246 LEU A CA  
1788 C  C   . LEU A 246 ? 0.8092 0.6697 0.7566 -0.0165 -0.0868 -0.0021 246 LEU A C   
1789 O  O   . LEU A 246 ? 0.8713 0.7250 0.8179 -0.0197 -0.0868 0.0019  246 LEU A O   
1790 C  CB  . LEU A 246 ? 0.7371 0.6022 0.6856 -0.0120 -0.0846 0.0018  246 LEU A CB  
1791 C  CG  . LEU A 246 ? 0.7873 0.6600 0.7382 -0.0111 -0.0830 0.0026  246 LEU A CG  
1792 C  CD1 . LEU A 246 ? 0.8683 0.7364 0.8160 -0.0069 -0.0824 0.0056  246 LEU A CD1 
1793 C  CD2 . LEU A 246 ? 0.7716 0.6532 0.7242 -0.0092 -0.0835 -0.0030 246 LEU A CD2 
1794 N  N   . GLU A 247 ? 0.8405 0.7014 0.7860 -0.0137 -0.0882 -0.0075 247 GLU A N   
1795 C  CA  . GLU A 247 ? 0.8511 0.7036 0.7927 -0.0142 -0.0898 -0.0089 247 GLU A CA  
1796 C  C   . GLU A 247 ? 0.8126 0.6553 0.7485 -0.0088 -0.0909 -0.0085 247 GLU A C   
1797 O  O   . GLU A 247 ? 0.8834 0.7160 0.8159 -0.0109 -0.0916 -0.0059 247 GLU A O   
1798 C  CB  . GLU A 247 ? 0.8177 0.6738 0.7592 -0.0144 -0.0905 -0.0145 247 GLU A CB  
1799 CL CL  . CL  B .   ? 0.5711 0.5470 0.5410 -0.0549 -0.0637 -0.0468 301 CL  A CL  
1800 C  C1  . EDO C .   ? 0.6057 0.4974 0.4926 -0.0919 -0.0462 0.0138  302 EDO A C1  
1801 O  O1  . EDO C .   ? 0.5289 0.4241 0.4161 -0.0948 -0.0442 0.0086  302 EDO A O1  
1802 C  C2  . EDO C .   ? 0.5551 0.4521 0.4514 -0.0879 -0.0488 0.0161  302 EDO A C2  
1803 O  O2  . EDO C .   ? 0.4989 0.3985 0.3996 -0.0850 -0.0479 0.0160  302 EDO A O2  
1804 C  C1  . EDO D .   ? 0.6037 0.5312 0.5864 -0.0879 -0.0933 0.0323  303 EDO A C1  
1805 O  O1  . EDO D .   ? 0.5482 0.4772 0.5304 -0.0900 -0.0957 0.0345  303 EDO A O1  
1806 C  C2  . EDO D .   ? 0.5424 0.4725 0.5306 -0.0850 -0.0909 0.0359  303 EDO A C2  
1807 O  O2  . EDO D .   ? 0.7802 0.7128 0.7742 -0.0866 -0.0933 0.0402  303 EDO A O2  
1808 N  N1  . IMD E .   ? 0.8033 0.6351 0.6524 -0.0445 -0.0249 0.0429  304 IMD A N1  
1809 C  C2  . IMD E .   ? 0.7609 0.5970 0.6155 -0.0440 -0.0264 0.0455  304 IMD A C2  
1810 N  N3  . IMD E .   ? 1.0634 0.8923 0.9119 -0.0412 -0.0252 0.0491  304 IMD A N3  
1811 C  C4  . IMD E .   ? 0.8459 0.6654 0.6848 -0.0399 -0.0228 0.0487  304 IMD A C4  
1812 C  C5  . IMD E .   ? 0.7936 0.6152 0.6331 -0.0421 -0.0226 0.0448  304 IMD A C5  
1813 C  C1  . EDO F .   ? 0.8894 0.7940 0.8464 -0.0007 -0.0162 0.0892  305 EDO A C1  
1814 O  O1  . EDO F .   ? 0.8331 0.7383 0.7919 0.0039  -0.0122 0.0938  305 EDO A O1  
1815 C  C2  . EDO F .   ? 0.8664 0.7778 0.8315 -0.0040 -0.0195 0.0899  305 EDO A C2  
1816 O  O2  . EDO F .   ? 0.9234 0.8396 0.8954 -0.0071 -0.0215 0.0894  305 EDO A O2  
# 
